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Science 15 December 1995:
Vol. 270. no. 5243, pp. 1821 - 1824
DOI: 10.1126/science.270.5243.1821
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Reports

Crystal Structure of the V Domain of a T Cell Antigen Receptor

Barry A. Fields,  Bertram Ober,  Emilio L. Malchiodi,  Marina I. Lebedeva,  Bradford C. Braden,  Xavier Ysern,  Jin-Kyoo Kim,  Xuguang Shao,  E. Sally Ward,  Roy A. Mariuzza (1)

The crystal structure of the V 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 beta sheet to the other enables a pair of V 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 association, a model of an (alphabeta)2 TCR tetramer can be positioned relative to the major histocompatibility complex class II (alphabeta)2 tetramer with the third hypervariable loop of V over the amino-terminal portion of the antigenic peptide and the corresponding loop of V over its carboxyl-terminal residues. TCR dimerization that is mediated by the alpha chain may contribute to the coupling of antigen recognition to signal transduction during T cell activation.


B. A. Fields, E. L. Malchiodi, M. I. Lebedeva, B. C. Braden, R. A. Mariuzza, Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850, USA.
B. Ober, J.-K. Kim, X. Shao, E. S. Ward, Cancer Immunobiology Center and Department of Microbiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75235-8576, USA.
X. Ysern, Center for Drug Evaluation and Research, U.S. Food and Drug Administration, 5600 Fishers Lane, Rockville, MD 20857, USA.
(1) To whom correspondence should be addressed.


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