2ckb
From Proteopedia
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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 Wed Nov 21 09:09:06 2007
