1MI5
The crystal structure of LC13 TcR in complex with HLAB8-EBV peptide complex
Summary for 1MI5
Entry DOI | 10.2210/pdb1mi5/pdb |
Related | 1KGC 1M05 |
Descriptor | MHC heavy chain, beta 2 microglobulin, Epstein Barr Virus peptide, ... (6 entities in total) |
Functional Keywords | t cell receptor, major histocompatability complex (class i), hla b8, epstein barr virus, immunodominant tcr (lc13), immune system |
Biological source | Homo sapiens (human) More |
Cellular location | Membrane; Single-pass type I membrane protein: P30460 Secreted: P61769 Membrane; Single-pass membrane protein (Potential): P01848 P01850 |
Total number of polymer chains | 5 |
Total formula weight | 94288.21 |
Authors | Kjer-Nielsen, L.,Clements, C.S.,Purcell, A.W.,Brooks, A.G.,Whisstock, J.C.,Burrows, S.R.,McCluskey, J.,Rossjohn, J. (deposition date: 2002-08-21, release date: 2003-02-04, Last modification date: 2024-04-03) |
Primary citation | Kjer-Nielsen, L.,Clements, C.S.,Purcell, A.W.,Brooks, A.G.,Whisstock, J.C.,Burrows, S.R.,McCluskey, J.,Rossjohn, J. A Structural Basis for the Selection of Dominant alphabeta T Cell Receptors in Antiviral Immunity IMMUNITY, 18:53-64, 2003 Cited by PubMed Abstract: We have examined the basis for immunodominant or "public" TCR usage in an antiviral CTL response. Residues encoded by each of the highly selected genetic elements of an immunodominant clonotype recognizing Epstein-Barr virus were critical to the antigen specificity of the receptor. Upon recognizing antigen, the immunodominant TCR undergoes extensive conformational changes in the complementarity determining regions (CDRs), including the disruption of the canonical structures of the germline-encoded CDR1alpha and CDR2alpha loops to produce an enhanced fit with the HLA-peptide complex. TCR ligation induces conformational changes in the TCRalpha constant domain thought to form part of the docking site for CD3epsilon. These findings indicate that TCR immunodominance is associated with structural properties conferring receptor specificity and suggest a novel structural link between TCR ligation and intracellular signaling. PubMed: 12530975DOI: 10.1016/S1074-7613(02)00513-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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