1DN2

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

Summary for 1DN2

• Entry DOI: 10.2210/pdb1dn2/pdb
• Descriptor: IMMUNOGLOBULIN LAMBDA HEAVY CHAIN, ENGINEERED PEPTIDE, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: fc igg phage display peptide, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 53065.46

Authors

DeLano, W.L.,Ultsch, M.H.,de Vos, A.M.,Wells, J.A. (deposition date: 1999-12-15, release date: 2000-05-17, Last modification date: 2024-10-30)

Primary citation

DeLano, W.L.,Ultsch, M.H.,de Vos, A.M.,Wells, J.A.
Convergent solutions to binding at a protein-protein interface.
Science, 287:1279-1283, 2000

PubMed Abstract: 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.

PubMed: 10678837
DOI: 10.1126/science.287.5456.1279

Experimental method

X-RAY DIFFRACTION (2.7 Å)