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dc.contributor.authorZhou, Bo
dc.contributor.authorChen, Qiang
dc.contributor.authorMallis, Robert J.
dc.contributor.authorZhang, Hongmin
dc.contributor.authorLiu, Jin-Huan
dc.contributor.authorReinherz, Ellis Leonard
dc.contributor.authorWang, Jiahuai
dc.date.accessioned2013-03-05T17:06:33Z
dc.date.issued2011
dc.identifier.citationZhou, Bo, Qiang Chen, Robert J. Mallis, Hongmin Zhang, Jin-huan Liu, Ellis L. Reinherz, and Jia-huai Wang. 2011. A conserved hydrophobic patch on V\(\beta\) domains revealed by TCR\(\beta\) chain crystal structures: Implications for pre-TCR dimerization. Frontiers in Immunology 2:5.en_US
dc.identifier.issn1664-3224en_US
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:10364615
dc.description.abstractThe \(\alpha\beta\) T cell receptor (TCR) is a multimeric complex whose \(\beta\) chain plays a crucial role in thymocyte development as well as antigen recognition by mature T lymphocytes. We report here crystal structures of individual \(\beta\) subunits, termed N15\(\beta\) (V\(\beta\)5.2D\(\beta\)2J\(\beta\)2.6C\(\beta\)2) and N30\(\beta\) (V\(\beta\)13D\(\beta\)1J\(\beta\)1.1C\(\beta\)2), derived from two \(\alpha\beta\) TCRs specific for the immunodominant vesicular stomatitis virus octapeptide (VSV-8) bound to the murine H-2K\(^b\) MHC class I molecule. The crystal packing of the N15\(\beta\) structure reveals a homodimer formed through two V\(\beta\) domains. The V\(\beta\)/V\(\beta\) module is topologically very similar to the V\(\alpha\)/V\(\beta\) module in the N15\(\alpha\beta\) heterodimer. By contrast, in the N30\(\beta\) structure, the V\(\beta\) domain’s external hydrophobic CFG face is covered by the neighboring molecule’s C\(\beta\) 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 V\(\beta\) 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.en_US
dc.language.isoen_USen_US
dc.publisherFrontiers Research Foundationen_US
dc.relation.isversionofdoi:10.3389/fimmu.2011.00005en_US
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3341985/pdf/en_US
dash.licenseLAA
dc.subjectT cell receptoren_US
dc.subjectbeta chainen_US
dc.subjectcrystal structureen_US
dc.subjectpre-TCRen_US
dc.titleA Conserved Hydrophobic Patch on V\(\beta\) Domains Revealed by TCR\(\beta\) Chain Crystal Structures: Implications for Pre-TCR Dimerizationen_US
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden_US
dc.relation.journalFrontiers in Immunologyen_US
dash.depositing.authorReinherz, Ellis Leonard
dc.date.available2013-03-05T17:06:33Z
dc.identifier.doi10.3389/fimmu.2011.00005*
dash.contributor.affiliatedLiu, Jin-Huan
dash.contributor.affiliatedZhou, Bo
dash.contributor.affiliatedMallis, Robert
dash.contributor.affiliatedChen, Qian
dash.contributor.affiliatedReinherz, Ellis
dash.contributor.affiliatedWang, Jia-Huai


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