1jbf
From Proteopedia
|
Hairpin Peptide that Inhibits IgE Activity by Binding to the High Affinity IgE Receptor
Overview
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.
About this Structure
1JBF is a Protein complex structure of sequences from [1] with ACE as ligand. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sat Nov 24 23:24:25 2007
