1rpq

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[[Image:1rpq.gif|left|200px]]
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{{STRUCTURE_1rpq| PDB=1rpq | SCENE= }}
{{STRUCTURE_1rpq| PDB=1rpq | SCENE= }}
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'''High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display'''
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===High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15242605 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15242605}}
==About this Structure==
==About this Structure==
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[[Category: Yin, J P.]]
[[Category: Yin, J P.]]
[[Category: Receptor/peptide complex]]
[[Category: Receptor/peptide complex]]
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Revision as of 03:27, 28 July 2008

Template:STRUCTURE 1rpq

High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta' Peptide from Phage Display

Template:ABSTRACT PUBMED 15242605

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

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