Crystal structure of the V_α domain of a T cell antigen receptor

Fields, Barry A., Ober, Bertram, Malchiodi, Emilio L., Lebedeva, Marina I., Braden, Bradford C., Ysern, Xavier, Kim, Jin Kyoo, Shao, Xuguang, Ward, E. Sally and Mariuzza, Roy A. (1995) Crystal structure of the V_α domain of a T cell antigen receptor. Science, 270 (5243), 1821. (doi:10.1126/science.270.5243.1821).

Abstract

The crystal structure of the V_α domain of a T cell antigen receptor (TCR) was determined at a resolution of 2.2 angstroms. This structure represents an immunoglobulin topology set different from those previously described. A switch in a polypeptide strand from one β sheet to the other enables a pair of V_α homodimers to pack together to form a tetramer, such that the homodimers are parallel to each other and all hypervariable loops face in one direction. On the basis of the observed mode of V_α association, a model of an (αβ)₂ TCR tetramer can be positioned relative to the major histocompatibility complex class II (αβ)₂ tetramer with the third hypervariable loop of V_α over the amino-terminal portion of the antigenic peptide and the corresponding loop of V_β over its carboxyl-terminal residues. TCR dimerization that is mediated by the α chain may contribute to the coupling of antigen recognition to signal transduction during T cell activation.

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Contributors

Author: E. Sally Ward

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