Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation.
Identifieur interne : 000106 ( Main/Exploration ); précédent : 000105; suivant : 000107Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation.
Auteurs : Maud Bernoux [Australie] ; Thomas Ve [Australie] ; Simon Williams [Australie] ; Christopher Warren [Australie] ; Danny Hatters [Australie] ; Eugene Valkov [Australie] ; Xiaoxiao Zhang [Australie] ; Jeffrey G. Ellis [Australie] ; Bostjan Kobe [Australie] ; Peter N. Dodds [Australie]Source :
- Cell host & microbe [ 1934-6069 ] ; 2011.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Basidiomycota (MeSH), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Homéostasie (MeSH), Lin (immunologie), Lin (microbiologie), Maladies des plantes (immunologie), Modèles moléculaires (MeSH), Motifs et domaines d'intéraction protéique (MeSH), Multimérisation de protéines (MeSH), Mutagenèse dirigée (MeSH), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (génétique), Protéines végétales (composition chimique), Protéines végétales (génétique), Simulation numérique (MeSH), Sites de fixation (MeSH), Structure quaternaire des protéines (MeSH), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Transduction du signal (MeSH).
- MESH :
- composition chimique : Protéines de fusion recombinantes, Protéines végétales.
- génétique : Protéines de fusion recombinantes, Protéines végétales.
- immunologie : Lin, Maladies des plantes.
- microbiologie : Lin.
- Alignement de séquences, Basidiomycota, Cristallographie aux rayons X, Données de séquences moléculaires, Homéostasie, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Multimérisation de protéines, Mutagenèse dirigée, Simulation numérique, Sites de fixation, Structure quaternaire des protéines, Structure secondaire des protéines, Séquence d'acides aminés, Transduction du signal.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Basidiomycota (MeSH), Binding Sites (MeSH), Computer Simulation (MeSH), Crystallography, X-Ray (MeSH), Flax (immunology), Flax (microbiology), Homeostasis (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Plant Diseases (immunology), Plant Proteins (chemistry), Plant Proteins (genetics), Protein Interaction Domains and Motifs (MeSH), Protein Multimerization (MeSH), Protein Structure, Quaternary (MeSH), Protein Structure, Secondary (MeSH), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Sequence Alignment (MeSH), Signal Transduction (MeSH).
- MESH :
- chemical , chemistry : Plant Proteins, Recombinant Fusion Proteins.
- chemical , genetics : Plant Proteins, Recombinant Fusion Proteins.
- immunology : Flax, Plant Diseases.
- microbiology : Flax.
- Amino Acid Sequence, Basidiomycota, Binding Sites, Computer Simulation, Crystallography, X-Ray, Homeostasis, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Secondary, Sequence Alignment, Signal Transduction.
Abstract
The Toll/interleukin-1 receptor (TIR) domain occurs in animal and plant immune receptors. In the animal Toll-like receptors, homodimerization of the intracellular TIR domain is required for initiation of signaling cascades leading to innate immunity. By contrast, the role of the TIR domain in cytoplasmic nucleotide-binding/leucine-rich repeat (NB-LRR) plant immune resistance proteins is poorly understood. L6 is a TIR-NB-LRR resistance protein from flax (Linum usitatissimum) that confers resistance to the flax rust phytopathogenic fungus (Melampsora lini). We determine the crystal structure of the L6 TIR domain and show that, although dispensable for pathogenic effector protein recognition, the TIR domain alone is both necessary and sufficient for L6 immune signaling. We demonstrate that the L6 TIR domain self-associates, most likely forming a homodimer. Analysis of the structure combined with site-directed mutagenesis suggests that self-association is a requirement for immune signaling and reveals distinct surface regions involved in self-association, signaling, and autoregulation.
DOI: 10.1016/j.chom.2011.02.009
PubMed: 21402359
PubMed Central: PMC3142617
Affiliations:
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Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072</wicri:regionArea><wicri:noRegion>Queensland 4072</wicri:noRegion></affiliation></author><author><name sortKey="Williams, Simon" sort="Williams, Simon" uniqKey="Williams S" first="Simon" last="Williams">Simon Williams</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072</wicri:regionArea><wicri:noRegion>Queensland 4072</wicri:noRegion></affiliation></author><author><name sortKey="Warren, Christopher" sort="Warren, Christopher" uniqKey="Warren C" first="Christopher" last="Warren">Christopher Warren</name><affiliation wicri:level="1"><nlm:affiliation>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601</wicri:regionArea><wicri:noRegion>Australian Capital Territory 2601</wicri:noRegion></affiliation></author><author><name sortKey="Hatters, Danny" sort="Hatters, Danny" uniqKey="Hatters D" first="Danny" last="Hatters">Danny Hatters</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria 3010, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria 3010</wicri:regionArea><orgName type="university">Université de Melbourne</orgName><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author><author><name sortKey="Valkov, Eugene" sort="Valkov, Eugene" uniqKey="Valkov E" first="Eugene" last="Valkov">Eugene Valkov</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072</wicri:regionArea><wicri:noRegion>Queensland 4072</wicri:noRegion></affiliation></author><author><name sortKey="Zhang, Xiaoxiao" sort="Zhang, Xiaoxiao" uniqKey="Zhang X" first="Xiaoxiao" last="Zhang">Xiaoxiao Zhang</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072</wicri:regionArea><wicri:noRegion>Queensland 4072</wicri:noRegion></affiliation></author><author><name sortKey="Ellis, Jeffrey G" sort="Ellis, Jeffrey G" uniqKey="Ellis J" first="Jeffrey G" last="Ellis">Jeffrey G. Ellis</name><affiliation wicri:level="1"><nlm:affiliation>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601</wicri:regionArea><wicri:noRegion>Australian Capital Territory 2601</wicri:noRegion></affiliation></author><author><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name><affiliation wicri:level="1"><nlm:affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia. Electronic address: b.kobe@uq.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072</wicri:regionArea><wicri:noRegion>Queensland 4072</wicri:noRegion></affiliation></author><author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name><affiliation wicri:level="1"><nlm:affiliation>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601, Australia. Electronic address: peter.dodds@csiro.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601</wicri:regionArea><wicri:noRegion>Australian Capital Territory 2601</wicri:noRegion></affiliation></author></analytic><series><title level="j">Cell host & microbe</title><idno type="eISSN">1934-6069</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Basidiomycota (MeSH)</term><term>Binding Sites (MeSH)</term><term>Computer Simulation (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Flax (immunology)</term><term>Flax (microbiology)</term><term>Homeostasis (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Plant Diseases (immunology)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (genetics)</term><term>Protein Interaction Domains and Motifs (MeSH)</term><term>Protein Multimerization (MeSH)</term><term>Protein Structure, Quaternary (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Sequence Alignment (MeSH)</term><term>Signal Transduction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Basidiomycota (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Homéostasie (MeSH)</term><term>Lin (immunologie)</term><term>Lin (microbiologie)</term><term>Maladies des plantes (immunologie)</term><term>Modèles moléculaires (MeSH)</term><term>Motifs et domaines d'intéraction protéique (MeSH)</term><term>Multimérisation de protéines (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Protéines de fusion recombinantes (composition chimique)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (génétique)</term><term>Simulation numérique (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Structure quaternaire des protéines (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plant Proteins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Plant Proteins</term><term>Recombinant Fusion Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines de fusion recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de fusion recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Lin</term><term>Maladies des plantes</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Flax</term><term>Plant Diseases</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Lin</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Flax</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Basidiomycota</term><term>Binding Sites</term><term>Computer Simulation</term><term>Crystallography, X-Ray</term><term>Homeostasis</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Protein Interaction Domains and Motifs</term><term>Protein Multimerization</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Sequence Alignment</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Basidiomycota</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Homéostasie</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Multimérisation de protéines</term><term>Mutagenèse dirigée</term><term>Simulation numérique</term><term>Sites de fixation</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Toll/interleukin-1 receptor (TIR) domain occurs in animal and plant immune receptors. In the animal Toll-like receptors, homodimerization of the intracellular TIR domain is required for initiation of signaling cascades leading to innate immunity. By contrast, the role of the TIR domain in cytoplasmic nucleotide-binding/leucine-rich repeat (NB-LRR) plant immune resistance proteins is poorly understood. L6 is a TIR-NB-LRR resistance protein from flax (Linum usitatissimum) that confers resistance to the flax rust phytopathogenic fungus (Melampsora lini). We determine the crystal structure of the L6 TIR domain and show that, although dispensable for pathogenic effector protein recognition, the TIR domain alone is both necessary and sufficient for L6 immune signaling. We demonstrate that the L6 TIR domain self-associates, most likely forming a homodimer. Analysis of the structure combined with site-directed mutagenesis suggests that self-association is a requirement for immune signaling and reveals distinct surface regions involved in self-association, signaling, and autoregulation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21402359</PMID><DateCompleted><Year>2011</Year><Month>07</Month><Day>01</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1934-6069</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>3</Issue><PubDate><Year>2011</Year><Month>Mar</Month><Day>17</Day></PubDate></JournalIssue><Title>Cell host & microbe</Title><ISOAbbreviation>Cell Host Microbe</ISOAbbreviation></Journal><ArticleTitle>Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation.</ArticleTitle><Pagination><MedlinePgn>200-211</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1931-3128(11)00065-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.chom.2011.02.009</ELocationID><Abstract><AbstractText>The Toll/interleukin-1 receptor (TIR) domain occurs in animal and plant immune receptors. In the animal Toll-like receptors, homodimerization of the intracellular TIR domain is required for initiation of signaling cascades leading to innate immunity. By contrast, the role of the TIR domain in cytoplasmic nucleotide-binding/leucine-rich repeat (NB-LRR) plant immune resistance proteins is poorly understood. L6 is a TIR-NB-LRR resistance protein from flax (Linum usitatissimum) that confers resistance to the flax rust phytopathogenic fungus (Melampsora lini). We determine the crystal structure of the L6 TIR domain and show that, although dispensable for pathogenic effector protein recognition, the TIR domain alone is both necessary and sufficient for L6 immune signaling. We demonstrate that the L6 TIR domain self-associates, most likely forming a homodimer. Analysis of the structure combined with site-directed mutagenesis suggests that self-association is a requirement for immune signaling and reveals distinct surface regions involved in self-association, signaling, and autoregulation.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bernoux</LastName><ForeName>Maud</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ve</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Williams</LastName><ForeName>Simon</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Warren</LastName><ForeName>Christopher</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hatters</LastName><ForeName>Danny</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Victoria 3010, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Valkov</LastName><ForeName>Eugene</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Xiaoxiao</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ellis</LastName><ForeName>Jeffrey G</ForeName><Initials>JG</Initials><AffiliationInfo><Affiliation>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kobe</LastName><ForeName>Bostjan</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience, Division of Chemistry and Structural Biology, University of Queensland, Brisbane, Queensland 4072, Australia; Centre for Infectious Disease Research, University of Queensland, Brisbane, Queensland 4072, Australia. Electronic address: b.kobe@uq.edu.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dodds</LastName><ForeName>Peter N</ForeName><Initials>PN</Initials><AffiliationInfo><Affiliation>CSIRO Plant Industry, Canberra, Australian Capital Territory 2601, Australia. Electronic address: peter.dodds@csiro.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM074265-01A2</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Cell Host Microbe</MedlineTA><NlmUniqueID>101302316</NlmUniqueID><ISSNLinking>1931-3128</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C095731">L6 protein, Linum usitatissimum</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003198" MajorTopicYN="N">Computer Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019597" MajorTopicYN="N">Flax</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="N">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020836" MajorTopicYN="N">Protein Structure, Quaternary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year><Month>10</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2010</Year><Month>12</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>02</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>3</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>3</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>7</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21402359</ArticleId><ArticleId IdType="pii">S1931-3128(11)00065-5</ArticleId><ArticleId IdType="doi">10.1016/j.chom.2011.02.009</ArticleId><ArticleId IdType="pmc">PMC3142617</ArticleId><ArticleId IdType="mid">NIHMS307075</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Curr Opin Plant Biol. 2009 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Ellis</name><name sortKey="Hatters, Danny" sort="Hatters, Danny" uniqKey="Hatters D" first="Danny" last="Hatters">Danny Hatters</name><name sortKey="Kobe, Bostjan" sort="Kobe, Bostjan" uniqKey="Kobe B" first="Bostjan" last="Kobe">Bostjan Kobe</name><name sortKey="Valkov, Eugene" sort="Valkov, Eugene" uniqKey="Valkov E" first="Eugene" last="Valkov">Eugene Valkov</name><name sortKey="Ve, Thomas" sort="Ve, Thomas" uniqKey="Ve T" first="Thomas" last="Ve">Thomas Ve</name><name sortKey="Warren, Christopher" sort="Warren, Christopher" uniqKey="Warren C" first="Christopher" last="Warren">Christopher Warren</name><name sortKey="Williams, Simon" sort="Williams, Simon" uniqKey="Williams S" first="Simon" last="Williams">Simon Williams</name><name sortKey="Zhang, Xiaoxiao" sort="Zhang, Xiaoxiao" uniqKey="Zhang X" first="Xiaoxiao" last="Zhang">Xiaoxiao Zhang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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