2KRI
Structure of a complex between domain V of beta2-glycoprotein I and the fourth ligand-binding module from LDLR determined with Haddock
Summary for 2KRI
| Entry DOI | 10.2210/pdb2kri/pdb |
| NMR Information | BMRB: 16639 |
| Descriptor | Beta-2-glycoprotein 1, Low-density lipoprotein receptor, CALCIUM ION (3 entities in total) |
| Functional Keywords | antiphospholipid syndrome, thrombosis, ldlr, receptor, disulfide bond, glycoprotein, heparin-binding, sushi, protein binding-endocytosis complex, protein binding/endocytosis |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 14017.92 |
| Authors | Beglova, N. (deposition date: 2009-12-18, release date: 2010-03-31, Last modification date: 2024-10-16) |
| Primary citation | 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 Cited by 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: 20223219DOI: 10.1016/j.str.2009.12.013 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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