1G4G

NMR STRUCTURE OF THE FIFTH DOMAIN OF HUMAN BETA2-GLYCOPROTEIN I

1G4G の概要

• エントリーDOI: 10.2210/pdb1g4g/pdb
• 関連するPDBエントリー: 1G4F
• 分子名称: BETA2-GLYCOPROTEIN I (1 entity in total)
• 機能のキーワード: short consensus repeat, sushi-domain, signaling protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9755.36

構造登録者

Hoshino, M.,Hagihara, Y.,Nishii, I.,Yamazaki, T.,Kato, H.,Goto, Y. (登録日: 2000-10-27, 公開日: 2000-11-15, 最終更新日: 2024-11-06)

主引用文献

Hoshino, M.,Hagihara, Y.,Nishii, I.,Yamazaki, T.,Kato, H.,Goto, Y.
Identification of the phospholipid-binding site of human beta(2)-glycoprotein I domain V by heteronuclear magnetic resonance.
J.Mol.Biol., 304:927-939, 2000

PubMed Abstract: To understand the mechanism of the interaction between human beta(2)-glycoprotein I (beta(2)-GPI) and negatively charged phospholipids, we determined the three-dimensional solution structure of the fifth domain of beta(2)-GPI by heteronuclear multidimensional NMR. The results showed that the molecule is composed of well-defined four anti-parallel beta-strands and two short alpha-helices, as well as a long highly flexible loop. Backbone dynamic analysis demonstrated significant mobility of the flexible loop on a subnanosecond time scale. Structural modeling of the nicked fifth domain, in which the Lys317-Thr318 peptide bond was specifically cleaved, revealed the importance of this long C-terminal loop for the interaction between beta(2)-GPI and negatively charged phospholipids. A titration experiment with the anionic surfactant SDS showed that this highly mobile loop, as well as the short beta-hairpin between betaC and betaD strands, which is rich in positively charged residues, specifically interact with the surfactant. The mobile loop, together with the surrounding positively charged residues, probably construct the binding site for negatively charged phospholipids such as cardiolipin.

PubMed: 11124037
DOI: 10.1006/jmbi.2000.4243

実験手法

SOLUTION NMR