1dn2: Difference between revisions

Revision as of 23:19, 30 June 2008

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File:1dn2.png

Template:STRUCTURE 1dn2

FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2

Template:ABSTRACT PUBMED 10678837

About this StructureAbout this Structure

1DN2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 Jun 30 23:19:20 2008

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-'''FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2'''
+===FC FRAGMENT OF HUMAN IGG1 IN COMPLEX WITH AN ENGINEERED 13 RESIDUE PEPTIDE DCAWHLGELVWCT-NH2===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10678837}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10678837 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10678837}}
 ==About this Structure==
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 [[Category: Wells, J A.]]
 [[Category: Fc igg phage display peptide]]
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