2KRI

Structure of a complex between domain V of beta2-glycoprotein I and the fourth ligand-binding module from LDLR determined with Haddock

2KRI の概要

• エントリーDOI: 10.2210/pdb2kri/pdb
• NMR情報: BMRB: 16639
• 分子名称: Beta-2-glycoprotein 1, Low-density lipoprotein receptor, CALCIUM ION (3 entities in total)
• 機能のキーワード: antiphospholipid syndrome, thrombosis, ldlr, receptor, disulfide bond, glycoprotein, heparin-binding, sushi, protein binding-endocytosis complex, protein binding/endocytosis
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 14017.92

構造登録者

Beglova, N. (登録日: 2009-12-18, 公開日: 2010-03-31, 最終更新日: 2024-10-16)

主引用文献

Lee, C.J.,De Biasio, A.,Beglova, N.
Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids.
Structure, 18:366-376, 2010

PubMed Abstract: Lipoprotein receptors of the LDLR family serve as clearance receptors for beta2GPI and as signaling receptors for the beta2GPI/antibody complexes in antiphospholipid syndrome. We compared four ligand-binding LA modules from LDLR and ApoER2 for their ability to bind domain V of beta2GPI (beta2GPI-DV). We found that the LA modules capable of binding beta2GPI-DV interact with the same region on beta2GPI-DV using residues at their calcium-coordination site. The structure of a complex between beta2GPI-DV and LA4 of LDLR, solved by molecular docking guided by NMR-derived restraints and extensively validated, represents the general mode of interaction between beta2GPI and lipoprotein receptors. We have shown that beta2GPI-DV cannot simultaneously bind to lipoprotein receptors and anionic phospholipids, suggesting that the association of beta2GPI/anti-beta2GPI antibody complexes with anionic phospholipids will interfere with lipoprotein receptors' signaling in APS.

PubMed: 20223219
DOI: 10.1016/j.str.2009.12.013

実験手法

SOLUTION NMR