Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes.
Identifieur interne : 002A28 ( PubMed/Checkpoint ); précédent : 002A27; suivant : 002A29Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes.
Auteurs : Gitte W. Haxholm [Danemark] ; Louise F. Nikolajsen [Danemark] ; Johan G. Olsen [Danemark] ; Jacob Fredsted [Danemark] ; Flemming H. Larsen [Danemark] ; Vincent Goffin [France] ; Stine F. Pedersen [Danemark] ; Andrew J. Brooks [Australie] ; Michael J. Waters [Australie] ; Birthe B. Kragelund [Danemark]Source :
- The Biochemical journal [ 1470-8728 ] ; 2015.
Descripteurs français
- KwdFr :
- Dichroïsme circulaire, Diffraction des rayons X, Diffusion aux petits angles, Double couche lipidique (), Double couche lipidique (métabolisme), Fragments peptidiques (), Fragments peptidiques (génétique), Fragments peptidiques (métabolisme), Humains, Interactions hydrophobes et hydrophiles, Lignée cellulaire, Membrane cellulaire (), Membrane cellulaire (métabolisme), Modèles moléculaires, Phosphatidylcholines (), Phosphatidylcholines (métabolisme), Phosphatidylsérine (), Phosphatidylsérine (métabolisme), Pliage des protéines, Protéines recombinantes (), Protéines recombinantes (métabolisme), Récepteur STH (), Récepteur STH (génétique), Récepteur STH (métabolisme), Récepteur prolactine (), Récepteur prolactine (génétique), Récepteur prolactine (métabolisme), Résonance magnétique nucléaire biomoléculaire, Structure tertiaire des protéines, Transduction du signal, Tyrosine (métabolisme).
- MESH :
- génétique : Fragments peptidiques, Récepteur STH, Récepteur prolactine.
- métabolisme : Double couche lipidique, Fragments peptidiques, Membrane cellulaire, Phosphatidylcholines, Phosphatidylsérine, Protéines recombinantes, Récepteur STH, Récepteur prolactine, Tyrosine.
- Dichroïsme circulaire, Diffraction des rayons X, Diffusion aux petits angles, Double couche lipidique, Fragments peptidiques, Humains, Interactions hydrophobes et hydrophiles, Lignée cellulaire, Membrane cellulaire, Modèles moléculaires, Phosphatidylcholines, Phosphatidylsérine, Pliage des protéines, Protéines recombinantes, Récepteur STH, Récepteur prolactine, Résonance magnétique nucléaire biomoléculaire, Structure tertiaire des protéines, Transduction du signal.
English descriptors
- KwdEn :
- Cell Line, Cell Membrane (chemistry), Cell Membrane (metabolism), Circular Dichroism, Humans, Hydrophobic and Hydrophilic Interactions, Lipid Bilayers (chemistry), Lipid Bilayers (metabolism), Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments (chemistry), Peptide Fragments (genetics), Peptide Fragments (metabolism), Phosphatidylcholines (chemistry), Phosphatidylcholines (metabolism), Phosphatidylserines (chemistry), Phosphatidylserines (metabolism), Protein Folding, Protein Structure, Tertiary, Receptors, Prolactin (chemistry), Receptors, Prolactin (genetics), Receptors, Prolactin (metabolism), Receptors, Somatotropin (chemistry), Receptors, Somatotropin (genetics), Receptors, Somatotropin (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Scattering, Small Angle, Signal Transduction, Tyrosine (metabolism), X-Ray Diffraction.
- MESH :
- chemical , chemistry : Lipid Bilayers, Peptide Fragments, Phosphatidylcholines, Phosphatidylserines, Receptors, Prolactin, Receptors, Somatotropin, Recombinant Proteins.
- chemistry : Cell Membrane.
- chemical , genetics : Peptide Fragments, Receptors, Prolactin, Receptors, Somatotropin.
- metabolism : Cell Membrane, Lipid Bilayers, Peptide Fragments, Phosphatidylcholines, Phosphatidylserines, Receptors, Prolactin, Receptors, Somatotropin, Recombinant Proteins, Tyrosine.
- Cell Line, Circular Dichroism, Humans, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Folding, Protein Structure, Tertiary, Scattering, Small Angle, Signal Transduction, X-Ray Diffraction.
Abstract
Class 1 cytokine receptors regulate essential biological processes through complex intracellular signalling networks. However, the structural platform for understanding their functions is currently incomplete as structure-function studies of the intracellular domains (ICDs) are critically lacking. The present study provides the first comprehensive structural characterization of any cytokine receptor ICD and demonstrates that the human prolactin (PRL) receptor (PRLR) and growth hormone receptor (GHR) ICDs are intrinsically disordered throughout their entire lengths. We show that they interact specifically with hallmark lipids of the inner plasma membrane leaflet through conserved motifs resembling immuno receptor tyrosine-based activation motifs (ITAMs). However, contrary to the observations made for ITAMs, lipid association of the PRLR and GHR ICDs was shown to be unaccompanied by changes in transient secondary structure and independent of tyrosine phosphorylation. The results of the present study provide a new structural platform for studying class 1 cytokine receptors and may implicate the membrane as an active component regulating intracellular signalling.
DOI: 10.1042/BJ20141243
PubMed: 25846210
Affiliations:
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Larsen</name><affiliation wicri:level="1"><nlm:affiliation>Department of Food Science, University of Copenhagen, 1958 Frederiksberg C, Denmark.</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Department of Food Science, University of Copenhagen, 1958 Frederiksberg C</wicri:regionArea><wicri:noRegion>1958 Frederiksberg C</wicri:noRegion></affiliation></author><author><name sortKey="Goffin, Vincent" sort="Goffin, Vincent" uniqKey="Goffin V" first="Vincent" last="Goffin">Vincent Goffin</name><affiliation wicri:level="1"><nlm:affiliation>Inserm, U1151, Institut Necker Enfants Malades (INEM), Equipe "Physiopathologie des hormones PRL/GH", 75993 Paris Cedex 14, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U1151, Institut Necker Enfants Malades (INEM), Equipe "Physiopathologie des hormones PRL/GH", 75993 Paris Cedex 14</wicri:regionArea><wicri:noRegion>75993 Paris Cedex 14</wicri:noRegion><wicri:noRegion>75993 Paris Cedex 14</wicri:noRegion></affiliation></author><author><name sortKey="Pedersen, Stine F" sort="Pedersen, Stine F" uniqKey="Pedersen S" first="Stine F" last="Pedersen">Stine F. Pedersen</name><affiliation wicri:level="1"><nlm:affiliation>Cell and Developmental Biology, Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark.</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Cell and Developmental Biology, Department of Biology, University of Copenhagen, 2200 Copenhagen</wicri:regionArea><placeName><settlement type="city">Copenhague</settlement><region type="région" nuts="2">Hovedstaden</region></placeName></affiliation></author><author><name sortKey="Brooks, Andrew J" sort="Brooks, Andrew J" uniqKey="Brooks A" first="Andrew J" last="Brooks">Andrew J. Brooks</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Molecular Bioscience, The University of Queensland, Qld 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute for Molecular Bioscience, The University of Queensland, Qld 4072</wicri:regionArea><wicri:noRegion>Qld 4072</wicri:noRegion></affiliation></author><author><name sortKey="Waters, Michael J" sort="Waters, Michael J" uniqKey="Waters M" first="Michael J" last="Waters">Michael J. Waters</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Molecular Bioscience, The University of Queensland, Qld 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Institute for Molecular Bioscience, The University of Queensland, Qld 4072</wicri:regionArea><wicri:noRegion>Qld 4072</wicri:noRegion></affiliation></author><author><name sortKey="Kragelund, Birthe B" sort="Kragelund, Birthe B" uniqKey="Kragelund B" first="Birthe B" last="Kragelund">Birthe B. Kragelund</name><affiliation wicri:level="1"><nlm:affiliation>Structural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark bbk@bio.ku.dk.</nlm:affiliation><country wicri:rule="url">Danemark</country><wicri:regionArea>Structural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, 2200 Copenhagen</wicri:regionArea><placeName><settlement type="city">Copenhague</settlement><region type="région" nuts="2">Hovedstaden</region></placeName></affiliation></author></analytic><series><title level="j">The Biochemical journal</title><idno type="eISSN">1470-8728</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line</term><term>Cell Membrane (chemistry)</term><term>Cell Membrane (metabolism)</term><term>Circular Dichroism</term><term>Humans</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Lipid Bilayers (chemistry)</term><term>Lipid Bilayers (metabolism)</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (genetics)</term><term>Peptide Fragments (metabolism)</term><term>Phosphatidylcholines (chemistry)</term><term>Phosphatidylcholines (metabolism)</term><term>Phosphatidylserines (chemistry)</term><term>Phosphatidylserines (metabolism)</term><term>Protein Folding</term><term>Protein Structure, Tertiary</term><term>Receptors, Prolactin (chemistry)</term><term>Receptors, Prolactin (genetics)</term><term>Receptors, Prolactin (metabolism)</term><term>Receptors, Somatotropin (chemistry)</term><term>Receptors, Somatotropin (genetics)</term><term>Receptors, Somatotropin (metabolism)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term><term>Scattering, Small Angle</term><term>Signal Transduction</term><term>Tyrosine (metabolism)</term><term>X-Ray Diffraction</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Dichroïsme circulaire</term><term>Diffraction des rayons X</term><term>Diffusion aux petits angles</term><term>Double couche lipidique ()</term><term>Double couche lipidique (métabolisme)</term><term>Fragments peptidiques ()</term><term>Fragments peptidiques (génétique)</term><term>Fragments peptidiques (métabolisme)</term><term>Humains</term><term>Interactions hydrophobes et hydrophiles</term><term>Lignée cellulaire</term><term>Membrane cellulaire ()</term><term>Membrane cellulaire (métabolisme)</term><term>Modèles moléculaires</term><term>Phosphatidylcholines ()</term><term>Phosphatidylcholines (métabolisme)</term><term>Phosphatidylsérine ()</term><term>Phosphatidylsérine (métabolisme)</term><term>Pliage des protéines</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (métabolisme)</term><term>Récepteur STH ()</term><term>Récepteur STH (génétique)</term><term>Récepteur STH (métabolisme)</term><term>Récepteur prolactine ()</term><term>Récepteur prolactine (génétique)</term><term>Récepteur prolactine (métabolisme)</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure tertiaire des protéines</term><term>Transduction du signal</term><term>Tyrosine (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lipid Bilayers</term><term>Peptide Fragments</term><term>Phosphatidylcholines</term><term>Phosphatidylserines</term><term>Receptors, Prolactin</term><term>Receptors, Somatotropin</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptide Fragments</term><term>Receptors, Prolactin</term><term>Receptors, Somatotropin</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Fragments peptidiques</term><term>Récepteur STH</term><term>Récepteur prolactine</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Lipid Bilayers</term><term>Peptide Fragments</term><term>Phosphatidylcholines</term><term>Phosphatidylserines</term><term>Receptors, Prolactin</term><term>Receptors, Somatotropin</term><term>Recombinant Proteins</term><term>Tyrosine</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Double couche lipidique</term><term>Fragments peptidiques</term><term>Membrane cellulaire</term><term>Phosphatidylcholines</term><term>Phosphatidylsérine</term><term>Protéines recombinantes</term><term>Récepteur STH</term><term>Récepteur prolactine</term><term>Tyrosine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Circular Dichroism</term><term>Humans</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Folding</term><term>Protein Structure, Tertiary</term><term>Scattering, Small Angle</term><term>Signal Transduction</term><term>X-Ray Diffraction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dichroïsme circulaire</term><term>Diffraction des rayons X</term><term>Diffusion aux petits angles</term><term>Double couche lipidique</term><term>Fragments peptidiques</term><term>Humains</term><term>Interactions hydrophobes et hydrophiles</term><term>Lignée cellulaire</term><term>Membrane cellulaire</term><term>Modèles moléculaires</term><term>Phosphatidylcholines</term><term>Phosphatidylsérine</term><term>Pliage des protéines</term><term>Protéines recombinantes</term><term>Récepteur STH</term><term>Récepteur prolactine</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure tertiaire des protéines</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Class 1 cytokine receptors regulate essential biological processes through complex intracellular signalling networks. However, the structural platform for understanding their functions is currently incomplete as structure-function studies of the intracellular domains (ICDs) are critically lacking. The present study provides the first comprehensive structural characterization of any cytokine receptor ICD and demonstrates that the human prolactin (PRL) receptor (PRLR) and growth hormone receptor (GHR) ICDs are intrinsically disordered throughout their entire lengths. We show that they interact specifically with hallmark lipids of the inner plasma membrane leaflet through conserved motifs resembling immuno receptor tyrosine-based activation motifs (ITAMs). However, contrary to the observations made for ITAMs, lipid association of the PRLR and GHR ICDs was shown to be unaccompanied by changes in transient secondary structure and independent of tyrosine phosphorylation. The results of the present study provide a new structural platform for studying class 1 cytokine receptors and may implicate the membrane as an active component regulating intracellular signalling.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25846210</PMID><DateCreated><Year>2015</Year><Month>08</Month><Day>26</Day></DateCreated><DateCompleted><Year>2015</Year><Month>10</Month><Day>06</Day></DateCompleted><DateRevised><Year>2015</Year><Month>08</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1470-8728</ISSN><JournalIssue CitedMedium="Internet"><Volume>468</Volume><Issue>3</Issue><PubDate><Year>2015</Year><Month>Jun</Month><Day>15</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem. J.</ISOAbbreviation></Journal><ArticleTitle>Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes.</ArticleTitle><Pagination><MedlinePgn>495-506</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1042/BJ20141243</ELocationID><Abstract><AbstractText>Class 1 cytokine receptors regulate essential biological processes through complex intracellular signalling networks. However, the structural platform for understanding their functions is currently incomplete as structure-function studies of the intracellular domains (ICDs) are critically lacking. The present study provides the first comprehensive structural characterization of any cytokine receptor ICD and demonstrates that the human prolactin (PRL) receptor (PRLR) and growth hormone receptor (GHR) ICDs are intrinsically disordered throughout their entire lengths. We show that they interact specifically with hallmark lipids of the inner plasma membrane leaflet through conserved motifs resembling immuno receptor tyrosine-based activation motifs (ITAMs). However, contrary to the observations made for ITAMs, lipid association of the PRLR and GHR ICDs was shown to be unaccompanied by changes in transient secondary structure and independent of tyrosine phosphorylation. The results of the present study provide a new structural platform for studying class 1 cytokine receptors and may implicate the membrane as an active component regulating intracellular signalling.</AbstractText><CopyrightInformation>© The Authors Journal compilation © 2015 Biochemical Society.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Haxholm</LastName><ForeName>Gitte W</ForeName><Initials>GW</Initials><AffiliationInfo><Affiliation>Structural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nikolajsen</LastName><ForeName>Louise F</ForeName><Initials>LF</Initials><AffiliationInfo><Affiliation>Structural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Olsen</LastName><ForeName>Johan G</ForeName><Initials>JG</Initials><AffiliationInfo><Affiliation>Structural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fredsted</LastName><ForeName>Jacob</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Cell and Developmental Biology, Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Larsen</LastName><ForeName>Flemming H</ForeName><Initials>FH</Initials><AffiliationInfo><Affiliation>Department of Food Science, University of Copenhagen, 1958 Frederiksberg C, Denmark.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Goffin</LastName><ForeName>Vincent</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Inserm, U1151, Institut Necker Enfants Malades (INEM), Equipe "Physiopathologie des hormones PRL/GH", 75993 Paris Cedex 14, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pedersen</LastName><ForeName>Stine F</ForeName><Initials>SF</Initials><AffiliationInfo><Affiliation>Cell and Developmental Biology, Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Brooks</LastName><ForeName>Andrew J</ForeName><Initials>AJ</Initials><AffiliationInfo><Affiliation>Institute for Molecular Bioscience, The University of Queensland, Qld 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Waters</LastName><ForeName>Michael J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Institute for Molecular Bioscience, The University of Queensland, Qld 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kragelund</LastName><ForeName>Birthe B</ForeName><Initials>BB</Initials><AffiliationInfo><Affiliation>Structural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, 2200 Copenhagen, Denmark bbk@bio.ku.dk.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>04</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008051">Lipid Bilayers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010713">Phosphatidylcholines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010718">Phosphatidylserines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011981">Receptors, Prolactin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011986">Receptors, Somatotropin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>40290-44-6</RegistryNumber><NameOfSubstance UI="C050294">1-palmitoyl-2-oleoylglycero-3-phosphoserine</NameOfSubstance></Chemical><Chemical><RegistryNumber>42HK56048U</RegistryNumber><NameOfSubstance UI="D014443">Tyrosine</NameOfSubstance></Chemical><Chemical><RegistryNumber>TE895536Y5</RegistryNumber><NameOfSubstance UI="C028694">1-palmitoyl-2-oleoylphosphatidylcholine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057927" MajorTopicYN="N">Hydrophobic and Hydrophilic Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008051" MajorTopicYN="N">Lipid Bilayers</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="Y">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010713" MajorTopicYN="N">Phosphatidylcholines</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010718" MajorTopicYN="N">Phosphatidylserines</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011981" MajorTopicYN="N">Receptors, Prolactin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011986" MajorTopicYN="N">Receptors, Somatotropin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053838" MajorTopicYN="N">Scattering, Small Angle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014443" MajorTopicYN="N">Tyrosine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014961" MajorTopicYN="N">X-Ray Diffraction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">growth hormone receptor</Keyword><Keyword MajorTopicYN="N">immuno T-cell receptor activation motifs</Keyword><Keyword MajorTopicYN="N">intrinsically disordered protein</Keyword><Keyword MajorTopicYN="N">membrane interaction</Keyword><Keyword MajorTopicYN="N">prolactin receptor</Keyword><Keyword MajorTopicYN="N">signalling</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>10</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>04</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>4</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>4</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>10</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25846210</ArticleId><ArticleId IdType="pii">BJ20141243</ArticleId><ArticleId IdType="doi">10.1042/BJ20141243</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>Danemark</li><li>France</li></country><region><li>Hovedstaden</li></region><settlement><li>Copenhague</li></settlement></list><tree><country name="Danemark"><region name="Hovedstaden"><name sortKey="Haxholm, Gitte W" sort="Haxholm, Gitte W" uniqKey="Haxholm G" first="Gitte W" last="Haxholm">Gitte W. Haxholm</name></region><name sortKey="Fredsted, Jacob" sort="Fredsted, Jacob" uniqKey="Fredsted J" first="Jacob" last="Fredsted">Jacob Fredsted</name><name sortKey="Kragelund, Birthe B" sort="Kragelund, Birthe B" uniqKey="Kragelund B" first="Birthe B" last="Kragelund">Birthe B. Kragelund</name><name sortKey="Larsen, Flemming H" sort="Larsen, Flemming H" uniqKey="Larsen F" first="Flemming H" last="Larsen">Flemming H. Larsen</name><name sortKey="Nikolajsen, Louise F" sort="Nikolajsen, Louise F" uniqKey="Nikolajsen L" first="Louise F" last="Nikolajsen">Louise F. Nikolajsen</name><name sortKey="Olsen, Johan G" sort="Olsen, Johan G" uniqKey="Olsen J" first="Johan G" last="Olsen">Johan G. Olsen</name><name sortKey="Pedersen, Stine F" sort="Pedersen, Stine F" uniqKey="Pedersen S" first="Stine F" last="Pedersen">Stine F. Pedersen</name></country><country name="France"><noRegion><name sortKey="Goffin, Vincent" sort="Goffin, Vincent" uniqKey="Goffin V" first="Vincent" last="Goffin">Vincent Goffin</name></noRegion></country><country name="Australie"><noRegion><name sortKey="Brooks, Andrew J" sort="Brooks, Andrew J" uniqKey="Brooks A" first="Andrew J" last="Brooks">Andrew J. Brooks</name></noRegion><name sortKey="Waters, Michael J" sort="Waters, Michael J" uniqKey="Waters M" first="Michael J" last="Waters">Michael J. Waters</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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