1KB5

MURINE T-CELL RECEPTOR VARIABLE DOMAIN/FAB COMPLEX

Summary for 1KB5

• Entry DOI: 10.2210/pdb1kb5/pdb
• Descriptor: KB5-C20 T-CELL ANTIGEN RECEPTOR, ANTIBODY DESIRE-1, ... (5 entities in total)
• Functional Keywords: t-cell receptor, strand switch, fab, anticlonotypic, (immunoglobulin/receptor), complex (immunoglobulin-receptor) complex, complex (immunoglobulin/receptor)
• Biological source: Mus musculus (house mouse); More
• Cellular location: Cell membrane ; Single-pass membrane protein : P01865
• Total number of polymer chains: 4
• Total formula weight: 73500.84

Authors

Housset, D.,Mazza, G.,Gregoire, C.,Piras, C.,Malissen, B.,Fontecilla-Camps, J.C. (deposition date: 1997-04-06, release date: 1998-04-08, Last modification date: 2024-11-20)

Primary citation

Housset, D.,Mazza, G.,Gregoire, C.,Piras, C.,Malissen, B.,Fontecilla-Camps, J.C.
The three-dimensional structure of a T-cell antigen receptor V alpha V beta heterodimer reveals a novel arrangement of the V beta domain.
EMBO J., 16:4205-4216, 1997

PubMed Abstract: The crystal structure of a mouse T-cell antigen receptor (TCR) Fv fragment complexed to the Fab fragment of a specific anti-clonotypic antibody has been determined to 2.6 A resolution. The polypeptide backbone of the TCR V alpha domain is very similar to those of other crystallographically determined V alphas, whereas the V beta structure is so far unique among TCR V beta domains in that it displays a switch of the c" strand from the inner to the outer beta-sheet. The beta chain variable region of this TCR antigen-binding site is characterized by a rather elongated third complementarity-determining region (CDR3beta) that packs tightly against the CDR3 loop of the alpha chain, without leaving any intervening hydrophobic pocket. Thus, the conformation of the CDR loops with the highest potential diversity distinguishes the structure of this TCR antigen-binding site from those for which crystallographic data are available. On the basis of all these results, we infer that a significant conformational change of the CDR3beta loop found in our TCR is required for binding to its cognate peptide-MHC ligand.

PubMed: 9250664
DOI: 10.1093/emboj/16.14.4205

Experimental method

X-RAY DIFFRACTION (2.5 Å)