2ckb

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[[Image:2ckb.gif|left|200px]]
[[Image:2ckb.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ckb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckb OCA], [http://www.ebi.ac.uk/pdbsum/2ckb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ckb RCSB]</span>
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'''STRUCTURE OF THE 2C/KB/DEV8 COMPLEX'''
'''STRUCTURE OF THE 2C/KB/DEV8 COMPLEX'''
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[[Category: Garcia, K C.]]
[[Category: Garcia, K C.]]
[[Category: Wilson, I A.]]
[[Category: Wilson, I A.]]
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[[Category: major histocompatibility complex]]
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[[Category: Major histocompatibility complex]]
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[[Category: t cell antigen receptor]]
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[[Category: T cell antigen receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:20:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:22:40 2008''
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Revision as of 19:20, 3 May 2008

Template:STRUCTURE 2ckb

STRUCTURE OF THE 2C/KB/DEV8 COMPLEX


Overview

The T cell receptor (TCR) inherently has dual specificity. T cells must recognize self-antigens in the thymus during maturation and then discriminate between foreign pathogens in the periphery. A molecular basis for this cross-reactivity is elucidated by the crystal structure of the alloreactive 2C TCR bound to self peptide-major histocompatibility complex (pMHC) antigen H-2Kb-dEV8 refined against anisotropic 3.0 angstrom resolution x-ray data. The interface between peptide and TCR exhibits extremely poor shape complementarity, and the TCR beta chain complementarity-determining region 3 (CDR3) has minimal interaction with the dEV8 peptide. Large conformational changes in three of the TCR CDR loops are induced upon binding, providing a mechanism of structural plasticity to accommodate a variety of different peptide antigens. Extensive TCR interaction with the pMHC alpha helices suggests a generalized orientation that is mediated by the Valpha domain of the TCR and rationalizes how TCRs can effectively "scan" different peptides bound within a large, low-affinity MHC structural framework for those that provide the slight additional kinetic stabilization required for signaling.

About this Structure

2CKB is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen., Garcia KC, Degano M, Pease LR, Huang M, Peterson PA, Teyton L, Wilson IA, Science. 1998 Feb 20;279(5354):1166-72. PMID:9469799 Page seeded by OCA on Sat May 3 22:20:57 2008

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