1rpq
From Proteopedia
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High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display
Overview
Two structurally distinct classes of peptides were recently identified by, phage display that bind the high-affinity IgE receptor, FcepsilonRI, and, block IgE binding and subsequent receptor activation. Both classes adopt, highly stable structures in solution, one forming a beta hairpin, with the, other forming a helical "zeta" structure. Despite these differences, the, two classes bind competitively to the same site on the receptor., Structural analyses of both peptide-receptor complexes by NMR spectroscopy, and/or X-ray crystallography reveal that the unrelated peptide scaffolds, have nevertheless converged to present a similar three-dimensional surface, to interact with FcepsilonRI and that their modes of interaction share a, key feature of the IgE-FcepsilonRI complex, the proline/tryptophan, sandwich.
About this Structure
1RPQ is a Single protein structure of sequence from Homo sapiens with NDG, SO4 and CIT as ligands. Full crystallographic information is available from OCA.
Reference
Convergent recognition of the IgE binding site on the high-affinity IgE receptor., Stamos J, Eigenbrot C, Nakamura GR, Reynolds ME, Yin J, Lowman HB, Fairbrother WJ, Starovasnik MA, Structure. 2004 Jul;12(7):1289-301. PMID:15242605
Page seeded by OCA on Mon Nov 12 19:06:16 2007
