3pqy | pdb_00003pqy

Crystal Structure of 6218 TCR in complex with the H2Db-PA224

spinqualitylabelsall models 3pqy, resolution 3.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pqy is a 20 chain structure with sequence from Homo sapiens, Mus musculus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.192Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B2MG_MOUSE Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Publication Abstract from PubMed Pathogen-specific responses are characterized by preferred profiles of peptide+class I MHC (pMHCI) glycoprotein-specific T-cell receptor (TCR) Variable (V)-region use. How TCRV-region bias impacts TCRalphabeta heterodimer selection and resultant diversity is unclear. The D(b)PA(224)-specific TCR repertoire in influenza A virus-infected C57BL/6J (B6) mice exhibits a preferred TCRV-region bias toward the TRBV29 gene segment and an optimal complementarity determining region (CDR3) beta-length of 6 aa. Despite these restrictions, D(b)PA(224)-specific BV29(+) T cells use a wide array of unique CDR3beta sequences. Structural characterization of a single, TRBV29(+)D(b)P(A224)-specific TCRalphabeta-pMHCI complex demonstrated that CDR3alpha amino acid side chains made specific peptide interactions, but the CDR3beta main chain exclusively contacted peptides. Thus, length but not amino acid sequence was key for recognition and flexibility in Vbeta-region use. In support of this hypothesis, retrovirus expression of the D(b)PA(224)-specific TCRValpha-chain was used to constrain pairing within a naive/immune epitope-specific repertoire. The retrogenic TCRValpha paired with a diversity of CDR3betas in the context of a preferred TCRVbeta spectrum. Overall, these data provide an explanation for the combination of TCRV region bias and diversity within selected repertoires, even as they maintain exquisite pMHCI specificity. Structural basis for enabling T-cell receptor diversity within biased virus-specific CD8+ T-cell responses.,Day EB, Guillonneau C, Gras S, La Gruta NL, Vignali DA, Doherty PC, Purcell AW, Rossjohn J, Turner SJ Proc Natl Acad Sci U S A. 2011 Jun 7;108(23):9536-41. Epub 2011 May 23. PMID:21606376 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures MHC 3D structures MHC I 3D structures

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