1i9e
From Proteopedia
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TCR DOMAIN
Overview
The T-cell receptor (TCR) is a heterodimeric cell-surface protein, consisting of two chains, alpha and beta, each of which is composed of a, variable (V) and a constant (C) domain. Crystals of the isolated V(alpha), domain of the murine TCR 2C were grown by serendipity from a solution, containing the extracellular domains of the intact TCR 2C and CD3 gamma, epsilon-chains. The V(alpha) crystal structure shows how crystal packing, can substitute for another V(alpha) domain in a different fashion from, that observed in V(alpha)/V(alpha) homodimer and V(alpha)/V(beta), heterodimer structures. Significant conformational changes occur in the, CDR3 and beta(3)beta(4) loops that normally form part of the dimer, interface. The monomeric V(alpha) domain provides the unique opportunity, to study the effect of dimerization on the conformation of the unliganded, complementarity-determining regions (CDR) of a TCR. This structure of an, individual V(alpha) module has implications for stability and, bioengineering of isolated antibody and immunoglobulin domains.
About this Structure
1I9E is a Single protein structure of sequence from Mus musculus with NAG as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of an isolated V(alpha) domain of the 2C T-cell receptor., Rudolph MG, Huang M, Teyton L, Wilson IA, J Mol Biol. 2001 Nov 16;314(1):1-8. PMID:11724527
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