2z35

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2z35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z35 OCA], [http://www.ebi.ac.uk/pdbsum/2z35 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2z35 RCSB]</span>
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[[Category: immune system]]
[[Category: immune system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:51:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:18:01 2008''

Revision as of 02:18, 31 March 2008


PDB ID 2z35

Drag the structure with the mouse to rotate
, resolution 2.2Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of immune receptor


Overview

All complexes of T cell receptors (TCRs) bound to peptide-major histocompatibility complex (pMHC) molecules assume a stereotyped binding 'polarity', despite wide variations in TCR-pMHC docking angles. However, existing TCR-pMHC crystal structures have failed to show broadly conserved pairwise interaction motifs. Here we determined the crystal structures of two TCRs encoded by the variable beta-chain 8.2 (V(beta)8.2), each bound to the MHC class II molecule I-A(u), and did energetic mapping of V(alpha) and V(beta) contacts with I-A(u). Together with two previously solved structures of V(beta)8.2-containing TCR-MHC complexes, we found four TCR-I-A complexes with structurally superimposable interactions between the V(beta) loops and the I-A alpha-helix. This examination of a narrow 'slice' of the TCR-MHC repertoire demonstrates what is probably one of many germline-derived TCR-MHC interaction 'codons'.

About this Structure

2Z35 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'., Feng D, Bond CJ, Ely LK, Maynard J, Garcia KC, Nat Immunol. 2007 Sep;8(9):975-83. Epub 2007 Aug 12. PMID:17694060

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