1kgc

Revision as of 18:44, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1kgc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kgc, resolution 1.5Å" /> '''Immune Receptor'''<b...)
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Immune Receptor

File:1kgc.gif


1kgc, resolution 1.5Å

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OverviewOverview

Despite a potential repertoire of >10(15) alphabeta T cell receptors, (TcR), the HLA B8-restricted cytolytic T cell response to a latent antigen, of Epstein-Barr virus (EBV) is strikingly limited in the TcR sequences, that are selected. Even in unrelated individuals this response is, dominated by a single highly restricted TcR clonotype that selects, identical combinations of hypervariable Valpha, Vbeta, D, J, and N region, genes. We have determined the 1.5 A crystal structure of this "public", TcR, revealing that five of the six hypervariable loops adopt novel, conformations providing a unique combining site that contains a deep, pocket predicted to overlay the HLA B8-peptide complex. The findings, suggest a structural basis for the immunodominance of this clonotype in, the immune response to EBV.

About this StructureAbout this Structure

1KGC is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The 1.5 A crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance., Kjer-Nielsen L, Clements CS, Brooks AG, Purcell AW, McCluskey J, Rossjohn J, Structure. 2002 Nov;10(11):1521-32. PMID:12429093

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