Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure.
Identifieur interne : 002949 ( Ncbi/Merge ); précédent : 002948; suivant : 002950Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure.
Auteurs : M. Nomizu [États-Unis] ; A. Otaka ; A. Utani ; P P Roller ; Y. YamadaSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1994.
Descripteurs français
- KwdFr :
- Cinétique, Conformation des protéines, Dichroïsme circulaire, Disulfures (métabolisme), Données de séquences moléculaires, Dénaturation des protéines, Fragments peptidiques (), Fragments peptidiques (métabolisme), Fragments peptidiques (synthèse chimique), Laminine (), Laminine (métabolisme), Stabilité de médicament, Structure secondaire des protéines, Structures macromoléculaires, Séquence d'acides aminés, Thermodynamique.
- MESH :
- métabolisme : Disulfures, Fragments peptidiques, Laminine.
- synthèse chimique : Fragments peptidiques.
- Cinétique, Conformation des protéines, Dichroïsme circulaire, Données de séquences moléculaires, Dénaturation des protéines, Fragments peptidiques, Laminine, Stabilité de médicament, Structure secondaire des protéines, Structures macromoléculaires, Séquence d'acides aminés, Thermodynamique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Circular Dichroism, Disulfides (metabolism), Drug Stability, Kinetics, Laminin (chemistry), Laminin (metabolism), Macromolecular Substances, Molecular Sequence Data, Peptide Fragments (chemical synthesis), Peptide Fragments (chemistry), Peptide Fragments (metabolism), Protein Conformation, Protein Denaturation, Protein Structure, Secondary, Thermodynamics.
- MESH :
- chemical , chemical synthesis : Peptide Fragments.
- chemical , chemistry : Laminin, Peptide Fragments.
- chemical , metabolism : Disulfides, Laminin, Peptide Fragments.
- Amino Acid Sequence, Circular Dichroism, Drug Stability, Kinetics, Macromolecular Substances, Molecular Sequence Data, Protein Conformation, Protein Denaturation, Protein Structure, Secondary, Thermodynamics.
Abstract
Laminin, a large multidomain glycoprotein specific to basement membranes, is a heterotrimer with alpha, beta, and gamma chains held together in an alpha-helical coiled-coil structure. Synthetic peptides comprising two 51-mers (B1 and B2) from the beta 1 and gamma 1 subunits and a 55-mer (M) from alpha 2 were used to study the molecular mechanisms in laminin chain assembly. Using the synthetic peptides in various mixing experiments, the heterotrimer (B1-B2-M) was preferentially produced. The thermal stability of the heterotrimer increased dramatically (by approximately 20 degrees C) over that of the B1-B2 heterodimer as measured by circular dichroism (CD) spectroscopy. The B1-B1 homodimer (Tm = 60 degrees C) showed higher thermal stability when compared to B1-B2 and B2-B2 dimers. However, the B1 + B2 mixture produced principally the B1-B2 heterodimer. These results suggested that the preferential formations of heterodimer was regulated by kinetic interactions between each chain. The B2 and M peptides have many hydrophobic isoleucine residues which were replaced by leucines. These substitutions were predicted to favor an alpha-helical conformation and a higher propensity for zipper formation. B2L and ML, in which all isoleucine residues were replaced by leucine, showed significantly increased alpha-helicities. While B2L was able to form heterodimers and heterotrimers similar to B2, ML was not able to participate in heterotrimer formation as efficiently as the M peptide. The thermal stability of B1-B2L was comparable to that of B1-B2, but B2L and/or ML containing trimers showed lower thermal stability than B1-B2-M. These results suggest that the isoleucine residues in the alpha 2 and gamma 1 chains are critical for stabilizing the heteromeric triple-stranded coiled-coil structure.
PubMed: 7982952
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Utani</name></author><author><name sortKey="Roller, P P" sort="Roller, P P" uniqKey="Roller P" first="P P" last="Roller">P P Roller</name></author><author><name sortKey="Yamada, Y" sort="Yamada, Y" uniqKey="Yamada Y" first="Y" last="Yamada">Y. Yamada</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:7982952</idno><idno type="pmid">7982952</idno><idno type="wicri:Area/PubMed/Corpus">002850</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002850</idno><idno type="wicri:Area/PubMed/Curation">002850</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002850</idno><idno type="wicri:Area/PubMed/Checkpoint">002752</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002752</idno><idno type="wicri:Area/Ncbi/Merge">002949</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure.</title><author><name sortKey="Nomizu, M" sort="Nomizu, M" uniqKey="Nomizu M" first="M" last="Nomizu">M. Nomizu</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Developmental Biology, NIDR, National Institutes of Health, Bethesda, Maryland 20892.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Laboratory of Developmental Biology, NIDR, National Institutes of Health, Bethesda</wicri:cityArea></affiliation></author><author><name sortKey="Otaka, A" sort="Otaka, A" uniqKey="Otaka A" first="A" last="Otaka">A. Otaka</name></author><author><name sortKey="Utani, A" sort="Utani, A" uniqKey="Utani A" first="A" last="Utani">A. Utani</name></author><author><name sortKey="Roller, P P" sort="Roller, P P" uniqKey="Roller P" first="P P" last="Roller">P P Roller</name></author><author><name sortKey="Yamada, Y" sort="Yamada, Y" uniqKey="Yamada Y" first="Y" last="Yamada">Y. Yamada</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Circular Dichroism</term><term>Disulfides (metabolism)</term><term>Drug Stability</term><term>Kinetics</term><term>Laminin (chemistry)</term><term>Laminin (metabolism)</term><term>Macromolecular Substances</term><term>Molecular Sequence Data</term><term>Peptide Fragments (chemical synthesis)</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (metabolism)</term><term>Protein Conformation</term><term>Protein Denaturation</term><term>Protein Structure, Secondary</term><term>Thermodynamics</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique</term><term>Conformation des protéines</term><term>Dichroïsme circulaire</term><term>Disulfures (métabolisme)</term><term>Données de séquences moléculaires</term><term>Dénaturation des protéines</term><term>Fragments peptidiques ()</term><term>Fragments peptidiques (métabolisme)</term><term>Fragments peptidiques (synthèse chimique)</term><term>Laminine ()</term><term>Laminine (métabolisme)</term><term>Stabilité de médicament</term><term>Structure secondaire des protéines</term><term>Structures macromoléculaires</term><term>Séquence d'acides aminés</term><term>Thermodynamique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Laminin</term><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Laminin</term><term>Peptide Fragments</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term><term>Fragments peptidiques</term><term>Laminine</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Fragments peptidiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Circular Dichroism</term><term>Drug Stability</term><term>Kinetics</term><term>Macromolecular Substances</term><term>Molecular Sequence Data</term><term>Protein Conformation</term><term>Protein Denaturation</term><term>Protein Structure, Secondary</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Conformation des protéines</term><term>Dichroïsme circulaire</term><term>Données de séquences moléculaires</term><term>Dénaturation des protéines</term><term>Fragments peptidiques</term><term>Laminine</term><term>Stabilité de médicament</term><term>Structure secondaire des protéines</term><term>Structures macromoléculaires</term><term>Séquence d'acides aminés</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Laminin, a large multidomain glycoprotein specific to basement membranes, is a heterotrimer with alpha, beta, and gamma chains held together in an alpha-helical coiled-coil structure. Synthetic peptides comprising two 51-mers (B1 and B2) from the beta 1 and gamma 1 subunits and a 55-mer (M) from alpha 2 were used to study the molecular mechanisms in laminin chain assembly. Using the synthetic peptides in various mixing experiments, the heterotrimer (B1-B2-M) was preferentially produced. The thermal stability of the heterotrimer increased dramatically (by approximately 20 degrees C) over that of the B1-B2 heterodimer as measured by circular dichroism (CD) spectroscopy. The B1-B1 homodimer (Tm = 60 degrees C) showed higher thermal stability when compared to B1-B2 and B2-B2 dimers. However, the B1 + B2 mixture produced principally the B1-B2 heterodimer. These results suggested that the preferential formations of heterodimer was regulated by kinetic interactions between each chain. The B2 and M peptides have many hydrophobic isoleucine residues which were replaced by leucines. These substitutions were predicted to favor an alpha-helical conformation and a higher propensity for zipper formation. B2L and ML, in which all isoleucine residues were replaced by leucine, showed significantly increased alpha-helicities. While B2L was able to form heterodimers and heterotrimers similar to B2, ML was not able to participate in heterotrimer formation as efficiently as the M peptide. The thermal stability of B1-B2L was comparable to that of B1-B2, but B2L and/or ML containing trimers showed lower thermal stability than B1-B2-M. These results suggest that the isoleucine residues in the alpha 2 and gamma 1 chains are critical for stabilizing the heteromeric triple-stranded coiled-coil structure.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7982952</PMID><DateCompleted><Year>1994</Year><Month>12</Month><Day>30</Day></DateCompleted><DateRevised><Year>2004</Year><Month>11</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>269</Volume><Issue>48</Issue><PubDate><Year>1994</Year><Month>Dec</Month><Day>02</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure.</ArticleTitle><Pagination><MedlinePgn>30386-92</MedlinePgn></Pagination><Abstract><AbstractText>Laminin, a large multidomain glycoprotein specific to basement membranes, is a heterotrimer with alpha, beta, and gamma chains held together in an alpha-helical coiled-coil structure. Synthetic peptides comprising two 51-mers (B1 and B2) from the beta 1 and gamma 1 subunits and a 55-mer (M) from alpha 2 were used to study the molecular mechanisms in laminin chain assembly. Using the synthetic peptides in various mixing experiments, the heterotrimer (B1-B2-M) was preferentially produced. The thermal stability of the heterotrimer increased dramatically (by approximately 20 degrees C) over that of the B1-B2 heterodimer as measured by circular dichroism (CD) spectroscopy. The B1-B1 homodimer (Tm = 60 degrees C) showed higher thermal stability when compared to B1-B2 and B2-B2 dimers. However, the B1 + B2 mixture produced principally the B1-B2 heterodimer. These results suggested that the preferential formations of heterodimer was regulated by kinetic interactions between each chain. The B2 and M peptides have many hydrophobic isoleucine residues which were replaced by leucines. These substitutions were predicted to favor an alpha-helical conformation and a higher propensity for zipper formation. B2L and ML, in which all isoleucine residues were replaced by leucine, showed significantly increased alpha-helicities. While B2L was able to form heterodimers and heterotrimers similar to B2, ML was not able to participate in heterotrimer formation as efficiently as the M peptide. The thermal stability of B1-B2L was comparable to that of B1-B2, but B2L and/or ML containing trimers showed lower thermal stability than B1-B2-M. These results suggest that the isoleucine residues in the alpha 2 and gamma 1 chains are critical for stabilizing the heteromeric triple-stranded coiled-coil structure.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nomizu</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Developmental Biology, NIDR, National Institutes of Health, Bethesda, Maryland 20892.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Otaka</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Utani</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Roller</LastName><ForeName>P P</ForeName><Initials>PP</Initials></Author><Author ValidYN="Y"><LastName>Yamada</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007797">Laminin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046911">Macromolecular Substances</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004355" MajorTopicYN="N">Drug Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007797" MajorTopicYN="N">Laminin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046911" MajorTopicYN="N">Macromolecular Substances</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="Y">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="Y">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>12</Month><Day>2</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>12</Month><Day>2</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>12</Month><Day>2</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7982952</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><noCountry><name sortKey="Otaka, A" sort="Otaka, A" uniqKey="Otaka A" first="A" last="Otaka">A. Otaka</name><name sortKey="Roller, P P" sort="Roller, P P" uniqKey="Roller P" first="P P" last="Roller">P P Roller</name><name sortKey="Utani, A" sort="Utani, A" uniqKey="Utani A" first="A" last="Utani">A. Utani</name><name sortKey="Yamada, Y" sort="Yamada, Y" uniqKey="Yamada Y" first="Y" last="Yamada">Y. Yamada</name></noCountry><country name="États-Unis"><region name="Maryland"><name sortKey="Nomizu, M" sort="Nomizu, M" uniqKey="Nomizu M" first="M" last="Nomizu">M. Nomizu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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