1kgc
From Proteopedia
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| - | [[Image:1kgc.gif|left|200px]] | + | [[Image:1kgc.gif|left|200px]] |
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| - | '''Immune Receptor''' | + | {{Structure |
| + | |PDB= 1kgc |SIZE=350|CAPTION= <scene name='initialview01'>1kgc</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Immune Receptor''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KGC is a [ | + | 1KGC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGC OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12429093 12429093] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: t-cell receptor]] | [[Category: t-cell receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:17:06 2008'' |
Revision as of 10:17, 20 March 2008
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| 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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