Download MendeleyCrystal structure of an isolated V(alpha) domain of the 2C T-cell receptor.
Rudolph, M.G., Huang, M., Teyton, L., Wilson, I.A.(2001) J Mol Biol 314: 1-8
- PubMed: 11724527
- DOI: https://doi.org/10.1006/jmbi.2001.5113
- Primary Citation of Related Structures:
1I9E - PubMed Abstract:
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.
Organizational Affiliation:
Department of Molecular Biology and Skaggs Institute for Chemical Biology (BCC-206), The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
