T-Cell Receptor
IUCr Abstract:
CRYSTALLIZATION OF MURINE T-CELL RECEPTORS
D. Williams , A. Heine, E.A. Stura, J. Snook and I.A. Wilson
Press Release
T-Cell receptor Structure
We thank E. Stura for advice and help with data collection and heavy atom screening;
T. Yeates, L. Pease, D. Kranz, H. Eisen, C. Scott, and R. Stefanko for discussions, materials, and assistance; N. H. Xuong for use of the UCSD X-ray facility; R. Lerner for constant encouragement and support; and M. Pique for production of figures. Supported by NIH RO1 CA58896 (I.A.W.) and NIH postdoctoral training grant T32-A107244 (K.C.G.) This is publication 10295-M from The Scripps Research Institute. The coordinates for 2C have been deposited in the Protein Data Bank (Brookhaven National Laboratory, Upton, NY) with accession code 1TCR.
Acknowledgement from:
An alpha/beta T Cell Receptor Structure at 2.5 Å and Its Orientation in the TCR-MHC
Complex. K. Christopher Garcia,
Massimo Degano, Robyn L. Stanfield, Anders Brunmark, Michael R. Jackson, Per A. Peterson, Luc Teyton, Ian A. Wilson Science 274 (1996)
The central event in the cellular immune response to invading microorganisms is the specific recognition offoreign peptides bound to major histocompatibility complex (MHC) molecules by the alpha/beta T cell receptor (TCR). The x-ray structure of the complete extracellular fragment of a glycosylated TCR was determined at 2.5 angstroms, and its orientation bound to a class I MHC-peptide (pMHC) complex was elucidated from crystals of the TCR-pMHC complex. The TCR resembles an antibody in the variable V-alpha and V-beta domains but deviates in the constant C-alpha domain and in the interdomain pairing of C-alpha with C-beta. Four of seven possible asparagine-linked glycosylation sites have ordered carbohydrate moieties, one of which lies in the C-alpha-C-beta interface. The TCR combining site is relatively flat except for a deep hydrophobic cavity between the hypervariable CDR3s (complementarity-determining regions) of the alpha and beta chains. The 2C TCR covers the class I MHC H-2Kb binding groove so that the V-alpha CDRs 1 and 2 are positioned over the amino-terminal region of the bound dEV8 peptide, the V-beta chain CDRs 1 and 2 are over the carboxyl-terminal region of the peptide,
and the V-alpha and V-beta CDR3s straddle the peptide between the helices around the central position of the peptide.
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Prior Work by: Massimo Degano