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1kgc
From Proteopedia
| 1kgc, resolution 1.50Å () | |||||||||
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| Domains: | V-set, DUF1968, IGv, IGc | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Immune Receptor
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1KGC is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Kjer-Nielsen L, Clements CS, Brooks AG, Purcell AW, McCluskey J, Rossjohn J. The 1.5 A crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance. Structure. 2002 Nov;10(11):1521-32. PMID:12429093
Page seeded by OCA on Tue Feb 17 00:17:06 2009

