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Article: A conserved hydrophobic patch on Vβ domains revealed by TCRβ chain crystal structures: implications for pre-TCR dimerization
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TitleA conserved hydrophobic patch on Vβ domains revealed by TCRβ chain crystal structures: implications for pre-TCR dimerization
 
AuthorsZhou, B
Chen, Q
Mallis, RJ
Zhang, H
Liu, JH
Reinherz, EL
Wang, JH
 
KeywordsT cell receptor
Beta chain
Crystal structure
Pre-TCR
 
Issue Date2011
 
PublisherFrontiers Research Foundation. The Journal's web site is located at http://www.frontiersin.org/immunology
 
CitationFrontiers in Immunology, 2011, v. 2 article no. 5 [How to Cite?]
DOI: http://dx.doi.org/10.3389/fimmu.2011.00005
 
AbstractThe αβ T cell receptor (TCR) is a multimeric complex whose β chain plays a crucial role in thymocyte development as well as antigen recognition by mature T lymphocytes. We report here crystal structures of individual β subunits, termed N15β (Vβ5.2Dβ2Jβ2.6Cβ2) and N30β (Vβ13Dβ1Jβ1.1Cβ2), derived from two αβ TCRs specific for the immunodominant vesicular stomatitis virus octapeptide (VSV-8) bound to the murine H-2Kb MHC class I molecule. The crystal packing of the N15β structure reveals a homodimer formed through two Vβ domains. The Vβ/Vβ module is topologically very similar to the Vα/Vβ module in the N15αβ heterodimer. By contrast, in the N30β structure, the Vβ domain’s external hydrophobic CFG face is covered by the neighboring molecule’s Cβ domain. In conjunction with systematic investigation of previously published TCR single-subunit structures, we identified several conserved residues forming a concave hydrophobic patch at the center of the CFG outer face of the Vβ and other V-type Ig-like domains. This hydrophobic patch is shielded from solvent exposure in the crystal packing, implying that it is unlikely to be thermodynamically stable if exposed on the thymocyte surface. Accordingly, we propose a dimeric pre-TCR model distinct from those suggested previously by others and discuss its functional and structural implications.
 
ISSN1664-3224
 
DOIhttp://dx.doi.org/10.3389/fimmu.2011.00005
 
DC FieldValue
dc.contributor.authorZhou, B
 
dc.contributor.authorChen, Q
 
dc.contributor.authorMallis, RJ
 
dc.contributor.authorZhang, H
 
dc.contributor.authorLiu, JH
 
dc.contributor.authorReinherz, EL
 
dc.contributor.authorWang, JH
 
dc.date.accessioned2011-05-11T08:31:42Z
 
dc.date.available2011-05-11T08:31:42Z
 
dc.date.issued2011
 
dc.description.abstractThe αβ T cell receptor (TCR) is a multimeric complex whose β chain plays a crucial role in thymocyte development as well as antigen recognition by mature T lymphocytes. We report here crystal structures of individual β subunits, termed N15β (Vβ5.2Dβ2Jβ2.6Cβ2) and N30β (Vβ13Dβ1Jβ1.1Cβ2), derived from two αβ TCRs specific for the immunodominant vesicular stomatitis virus octapeptide (VSV-8) bound to the murine H-2Kb MHC class I molecule. The crystal packing of the N15β structure reveals a homodimer formed through two Vβ domains. The Vβ/Vβ module is topologically very similar to the Vα/Vβ module in the N15αβ heterodimer. By contrast, in the N30β structure, the Vβ domain’s external hydrophobic CFG face is covered by the neighboring molecule’s Cβ domain. In conjunction with systematic investigation of previously published TCR single-subunit structures, we identified several conserved residues forming a concave hydrophobic patch at the center of the CFG outer face of the Vβ and other V-type Ig-like domains. This hydrophobic patch is shielded from solvent exposure in the crystal packing, implying that it is unlikely to be thermodynamically stable if exposed on the thymocyte surface. Accordingly, we propose a dimeric pre-TCR model distinct from those suggested previously by others and discuss its functional and structural implications.
 
dc.description.naturepublished_or_final_version
 
dc.identifier.citationFrontiers in Immunology, 2011, v. 2 article no. 5 [How to Cite?]
DOI: http://dx.doi.org/10.3389/fimmu.2011.00005
 
dc.identifier.doihttp://dx.doi.org/10.3389/fimmu.2011.00005
 
dc.identifier.hkuros184808
 
dc.identifier.issn1664-3224
 
dc.identifier.issue5
 
dc.identifier.openurl
 
dc.identifier.urihttp://hdl.handle.net/10722/133327
 
dc.identifier.volume2
 
dc.languageeng
 
dc.publisherFrontiers Research Foundation. The Journal's web site is located at http://www.frontiersin.org/immunology
 
dc.relation.ispartofFrontiers in Immunology
 
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License
 
dc.rightsThis Document is Protected by copyright and was first published by Frontiers. All rights reserved. It is reproduced with permission.
 
dc.subjectT cell receptor
 
dc.subjectBeta chain
 
dc.subjectCrystal structure
 
dc.subjectPre-TCR
 
dc.titleA conserved hydrophobic patch on Vβ domains revealed by TCRβ chain crystal structures: implications for pre-TCR dimerization
 
dc.typeArticle
 
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