1dn2
From Proteopedia
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FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2
Contents |
Overview
The hinge region on the Fc fragment of human immunoglobulin G interacts, with at least four different natural protein scaffolds that bind at a, common site between the C(H2) and C(H3) domains. This "consensus" site was, also dominant for binding of random peptides selected in vitro for high, affinity (dissociation constant, about 25 nanomolar) by bacteriophage, display. Thus, this site appears to be preferred owing to its intrinsic, physiochemical properties, and not for biological function alone. A 2.7, angstrom crystal structure of a selected 13-amino acid peptide in complex, with Fc demonstrated that the peptide adopts a compact structure radically, different from that of the other Fc binding proteins. Nevertheless, the, specific Fc binding interactions of the peptide strongly mimic those of, the other proteins. Juxtaposition of the available Fc-complex crystal, structures showed that the convergent binding surface is highly, accessible, adaptive, and hydrophobic and contains relatively few sites, for polar interactions. These are all properties that may promote, cross-reactive binding, which is common to protein-protein interactions, and especially hormone-receptor complexes.
Disease
Known disease associated with this structure: Agammaglobulinemia OMIM:[147020]
About this Structure
1DN2 is a Single protein structure of sequence from Homo sapiens with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Convergent solutions to binding at a protein-protein interface., DeLano WL, Ultsch MH, de Vos AM, Wells JA, Science. 2000 Feb 18;287(5456):1279-83. PMID:10678837
Page seeded by OCA on Mon Nov 12 16:34:00 2007
