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Article: A conserved hydrophobic patch on Vβ domains revealed by TCRβ chain crystal structures: implications for pre-TCR dimerization

TitleA conserved hydrophobic patch on Vβ domains revealed by TCRβ chain crystal structures: implications for pre-TCR dimerization
Authors
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
Citation
Frontiers in Immunology, 2011, v. 2 article no. 5 How to Cite?
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.
Persistent Identifierhttp://hdl.handle.net/10722/133327
ISSN

 

DC FieldValueLanguage
dc.contributor.authorZhou, Ben_US
dc.contributor.authorChen, Qen_US
dc.contributor.authorMallis, RJen_US
dc.contributor.authorZhang, Hen_US
dc.contributor.authorLiu, JHen_US
dc.contributor.authorReinherz, ELen_US
dc.contributor.authorWang, JHen_US
dc.date.accessioned2011-05-11T08:31:42Z-
dc.date.available2011-05-11T08:31:42Z-
dc.date.issued2011en_US
dc.identifier.citationFrontiers in Immunology, 2011, v. 2 article no. 5en_US
dc.identifier.issn1664-3224en_US
dc.identifier.urihttp://hdl.handle.net/10722/133327-
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.languageengen_US
dc.publisherFrontiers Research Foundation. The Journal's web site is located at http://www.frontiersin.org/immunology-
dc.relation.ispartofFrontiers in Immunologyen_US
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 dimerizationen_US
dc.typeArticleen_US
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1664-3224&volume=2&issue=5&spage=&epage=&date=2011&atitle=A+conserved+hydrophobic+patch+on+Vβ+domains+revealed+by+TCRβ+chain+crystal+structures:+implications+for+pre-TCR+dimerizationen_US
dc.identifier.emailZhang, H: hzhang20@hku.hken_US
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.3389/fimmu.2011.00005-
dc.identifier.hkuros184808en_US
dc.identifier.volume2en_US
dc.identifier.issue5-

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