1KGC

Immune Receptor

Summary for 1KGC

• Entry DOI: 10.2210/pdb1kgc/pdb
• Descriptor: T-cell receptor alpha chain, T-cell receptor beta chain (3 entities in total)
• Functional Keywords: t-cell receptor, lc13 clone, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass membrane protein (Potential): P01848 P01850
• Total number of polymer chains: 2
• Total formula weight: 50165.59

Authors

Kjer-Nielsen, L.,Clements, C.S.,Brooks, A.G.,Purcell, A.W.,McCluskey, J.,Rossjohn, J. (deposition date: 2001-11-26, release date: 2002-12-11, Last modification date: 2022-12-21)

Primary citation

Kjer-Nielsen, L.,Clements, C.S.,Brooks, A.G.,Purcell, A.W.,McCluskey, J.,Rossjohn, J.
The 1.5 A crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance
STRUCTURE, 10:1521-1532, 2002

PubMed Abstract: Despite a potential repertoire of >10(15) alphabeta T cell receptors (TcR), the HLA B8-restricted cytolytic T cell response to a latent antigen of Epstein-Barr virus (EBV) is strikingly limited in the TcR sequences that are selected. Even in unrelated individuals this response is dominated by a single highly restricted TcR clonotype that selects identical combinations of hypervariable Valpha, Vbeta, D, J, and N region genes. We have determined the 1.5 A crystal structure of this "public" TcR, revealing that five of the six hypervariable loops adopt novel conformations providing a unique combining site that contains a deep pocket predicted to overlay the HLA B8-peptide complex. The findings suggest a structural basis for the immunodominance of this clonotype in the immune response to EBV.

PubMed: 12429093
DOI: 10.1016/S0969-2126(02)00878-X

Experimental method

X-RAY DIFFRACTION (1.5 Å)