1RPQ

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

Summary for 1RPQ

• Entry DOI: 10.2210/pdb1rpq/pdb
• Related: 1F2Q 1F6A 1KCO
• Related PRD ID: PRD_900017
• Descriptor: High affinity immunoglobulin epsilon receptor alpha-subunit precursor, Peptide E131, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: receptor-peptide complex, membrane protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 8
• Total formula weight: 101565.20

Authors

Stamos, J.,Eigenbrot, C.,Nakamura, G.R.,Reynolds, M.E.,Yin, J.P.,Lowman, H.B.,Fairbrother, W.J.,Starovasnik, M.A. (deposition date: 2003-12-03, release date: 2004-07-20, Last modification date: 2024-10-09)

Primary citation

Stamos, J.,Eigenbrot, C.,Nakamura, G.R.,Reynolds, M.E.,Yin, J.P.,Lowman, H.B.,Fairbrother, W.J.,Starovasnik, M.A.
Convergent Recognition of the IgE Binding Site on the High-Affinity IgE Receptor.
Structure, 12:1289-1301, 2004

PubMed Abstract: 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.

PubMed: 15242605
DOI: 10.1016/j.str.2004.04.015

Experimental method

X-RAY DIFFRACTION (3 Å)