1DN2

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

1DN2 の概要

• エントリーDOI: 10.2210/pdb1dn2/pdb
• 分子名称: 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)
• 機能のキーワード: fc igg phage display peptide, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 53065.46

構造登録者

DeLano, W.L.,Ultsch, M.H.,de Vos, A.M.,Wells, J.A. (登録日: 1999-12-15, 公開日: 2000-05-17, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.7 Å)