1rpq
From Proteopedia
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| , resolution 3.00Å | |||||||
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| Ligands: | , , , , | ||||||
| Gene: | FCER1A, FCE1A (Homo sapiens) | ||||||
| Related: | 1KCO, 1F2Q, 1F6A
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 23:31:17 2008
