1kgc
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kgc OCA], [http://www.ebi.ac.uk/pdbsum/1kgc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kgc RCSB]</span> | ||
}} | }} | ||
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[[Category: t-cell receptor]] | [[Category: t-cell receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:48:12 2008'' |
Revision as of 18:48, 30 March 2008
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| , resolution 1.5Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Immune Receptor
Overview
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 Structure
1KGC is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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