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Publication Abstract from PubMed

Alphabeta T-cell receptors (TcRs) play a central role in cellular immune response. They are members of the Ig superfamily, with extracellular regions of the alpha and beta chains each comprising a V-type domain and a C-type domain. We have determined the ectodomain structure of an alphabeta TcR, which recognizes the autoantigen myelin basic protein. The 2.0-A-resolution structure reveals canonical main-chain conformations for the V(alpha), V(beta), and C(beta) domains, but the C(alpha) domain exhibits a main-chain conformation remarkably different from those previously reported for TcR crystal structures. The global IgC-like fold is maintained, but a piston-like rearrangement between BC and DE beta-turns results in beta-strand slippage. This substantial conformational change may represent a signaling intermediate. Our structure is the first example for the Ig fold of the increasingly recognized concept of "metamorphic proteins."

An alternative conformation of the T-cell receptor alpha constant region.,van Boxel GI, Holmes S, Fugger L, Jones EY J Mol Biol. 2010 Jul 23;400(4):828-37. Epub 2010 May 31. PMID:20630474^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.