| Structural highlights
1rpq is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , ,
| | Related: | 1kco, 1f2q, 1f6a |
| Gene: | FCER1A, FCE1A (Homo sapiens) |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stamos J, Eigenbrot C, Nakamura GR, Reynolds ME, Yin J, Lowman HB, Fairbrother WJ, Starovasnik MA. Convergent recognition of the IgE binding site on the high-affinity IgE receptor. Structure. 2004 Jul;12(7):1289-301. PMID:15242605 doi:10.1016/j.str.2004.04.015
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