1IOD
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE COAGULATION FACTOR X BINDING PROTEIN FROM SNAKE VENOM AND THE GLA DOMAIN OF FACTOR X
Summary for 1IOD
| Entry DOI | 10.2210/pdb1iod/pdb |
| Related | 1BJ3 1IXX |
| Descriptor | COAGULATION FACTOR X BINDING PROTEIN, COAGULATION FACTOR X GLA DOMAIN, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | calcium bridging, domain swapping, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Deinagkistrodon acutus (Chinese moccasin) More |
| Cellular location | Secreted: P00743 |
| Total number of polymer chains | 3 |
| Total formula weight | 35478.04 |
| Authors | Mizuno, H.,Fujimoto, Z.,Atoda, H.,Morita, T. (deposition date: 2001-02-27, release date: 2001-06-27, Last modification date: 2024-04-03) |
| Primary citation | Mizuno, H.,Fujimoto, Z.,Atoda, H.,Morita, T. Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X. Proc.Natl.Acad.Sci.Usa, 98:7230-7234, 2001 Cited by PubMed Abstract: The gamma-carboxyglutamic acid (Gla) domain of blood coagulation factors is responsible for Ca2+-dependent phospholipid membrane binding. Factor X-binding protein (X-bp), an anticoagulant protein from snake venom, specifically binds to the Gla domain of factor X. The crystal structure of X-bp in complex with the Gla domain peptide of factor X at 2.3-A resolution showed that the anticoagulation is based on the fact that two patches of the Gla domain essential for membrane binding are buried in the complex formation. The Gla domain thus is expected to be a new target of anticoagulant drugs, and X-bp provides a basis for designing them. This structure also provides a membrane-bound model of factor X. PubMed: 11404471DOI: 10.1073/pnas.131179698 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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