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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."

Original publication

DOI

10.1016/j.jmb.2010.05.053

Type

Journal article

Journal

J Mol Biol

Publication Date

23/07/2010

Volume

400

Pages

828 - 837

Keywords

Amino Acid Sequence, Animals, Crystallography, X-Ray, Mice, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Quaternary, Receptors, Antigen, T-Cell, alpha-beta