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|2ckb, resolution 3.00Å ()|
STRUCTURE OF THE 2C/KB/DEV8 COMPLEX
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Garcia KC, Degano M, Pease LR, Huang M, Peterson PA, Teyton L, Wilson IA. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science. 1998 Feb 20;279(5354):1166-72. PMID:9469799