TY - JOUR
AU - Mariuzza, R A
AB - The crystal structure of the V alpha 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 alpha 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 alpha association, a model of an (alpha beta)2 TCR tetramer can be positioned relative to the major histocompatibility complex class II (alpha beta)2 tetramer with the third hypervariable loop of V alpha over the amino-terminal portion of the antigenic peptide and the corresponding loop of V beta 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.
TI - Crystal structure of the V alpha domain of a T cell antigen receptor.
JF - Science (New York, N.Y.)
DO - 10.1126/science.270.5243.1821
DA - 1996-01-22
UR - https://www.deepdyve.com/lp/pubmed/crystal-structure-of-the-v-alpha-domain-of-a-t-cell-antigen-receptor-OCvGwUw9p0
SP - 1821
EP - 4
VL - 270
IS - 5243
DP - DeepDyve
ER -