1jbf

Hairpin Peptide that Inhibits IgE Activity by Binding to the High Affinity IgE Receptor

spinqualitylabelsall models 1jbf, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1jbf is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: ACE Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed A family of structured peptides that bind to FcepsilonRIalpha, the alpha-chain of the high-affinity receptor for IgE, has been identified. Binding selections using FcepsilonRIalpha and polyvalent peptide-phage libraries yielded a dominant 18-residue peptide-phage clone, as well as related sequences that did not resemble fragments of IgE. Synthetic peptides based on these sequences inhibited IgE binding to its receptor, and were found by NMR analysis to adopt a stable beta-hairpin structure in solution. Optimized peptides with micromolar receptor affinity exhibited high stability in biological fluids and inhibited cellular histamine release in an in vitro bioassay of IgE activity. The structure-activity relationships of these peptides, which are less than 1% of the size of IgE, suggest an overlap between their binding site and that of IgE on FcepsilonRI. Thus, the peptides demonstrate that blocking a small epitope on this receptor chain is sufficient to block IgE activity. Such structured peptides represent a possible starting point for the design of novel antagonists, and offer the potential for testing in vivo a new approach for treating allergic disease. A novel family of hairpin peptides that inhibit IgE activity by binding to the high-affinity IgE receptor.,Nakamura GR, Starovasnik MA, Reynolds ME, Lowman HB Biochemistry. 2001 Aug 21;40(33):9828-35. PMID:11502176 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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