An alternative conformation of the T-cell receptor alpha constant region.

Journal of Molecular Biology
Gijs I van BoxelE Yvonne Jones

Abstract

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."

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Citations

Nov 26, 2014·Proceedings of the National Academy of Sciences of the United States of America·Michael E BirnbaumK Christopher Garcia
Jun 16, 2017·Journal of Chemical Theory and Computation·Bernhard KnappCharlotte M Deane
Aug 26, 2018·Protein Science : a Publication of the Protein Society·Prakash KulkarniJohn Orban
May 17, 2017·Nature Communications·Kannan NatarajanNikolaos G Sgourakis
Nov 26, 2021·Journal of Biomolecular Structure & Dynamics·Junaida M IbrahimPerumana R Sudhakaran

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Methods Mentioned

BETA
transgenic
glycosylation
PCR
column
gel filtration
dynamic light scattering
X-ray

Software Mentioned

PROCHECK
GAP
HKL2000
Phaser
REFMAC

Related Concepts

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