1oga | pdb_00001oga
From Proteopedia
A STRUCTURAL BASIS FOR IMMUNODOMINANT HUMAN T-CELL RECEPTOR RECOGNITION.
| ||||||||||||
Structural highlights
Function[1A02_HUMAN] Involved in the presentation of foreign antigens to the immune system. Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe anti-influenza CD8+ T cell response in HLA-A2-positive adults is almost exclusively directed at residues 58-66 of the virus matrix protein (MP(58-66)). V(beta)17V(alpha)10.2 T cell receptors (TCRs) containing a conserved arginine-serine-serine sequence in complementarity determining region 3 (CDR3) of the V(beta) segment dominate this response. To investigate the molecular basis of immunodominant selection in an outbred population, we have determined the crystal structure of V(beta)17V(alpha)10.2 in complex with MP(58-66)-HLA-A2 at a resolution of 1.4 A. We show that, whereas the TCR typically fits over an exposed side chain of the peptide, in this structure MP(58-66) exposes only main chain atoms. This distinctive orientation of V(beta)17V(alpha)10.2, which is almost orthogonal to the peptide-binding groove of HLA-A2, facilitates insertion of the conserved arginine in V(beta) CDR3 into a notch in the surface of MP(58-66)-HLA-A2. This previously unknown binding mode underlies the immunodominant T cell response. A structural basis for immunodominant human T cell receptor recognition.,Stewart-Jones GB, McMichael AJ, Bell JI, Stuart DI, Jones EY Nat Immunol. 2003 Jul;4(7):657-63. Epub 2003 Jun 8. PMID:12796775[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||
This page was last modified 04:58, 10 February 2016.