1BX7
HIRUSTASIN FROM HIRUDO MEDICINALIS AT 1.2 ANGSTROMS
Summary for 1BX7
| Entry DOI | 10.2210/pdb1bx7/pdb |
| Descriptor | HIRUSTASIN, SULFATE ION (3 entities in total) |
| Functional Keywords | anti-coagulant, peptidic inhibitors, conformational flexibility, serine protease inhibitor |
| Biological source | Hirudo medicinalis (medicinal leech) |
| Cellular location | Secreted: P80302 |
| Total number of polymer chains | 1 |
| Total formula weight | 6078.91 |
| Authors | Uson, I.,Sheldrick, G.M.,De La Fortelle, E.,Bricogne, G.,Di Marco, S.,Priestle, J.P.,Gruetter, M.G.,Mittl, P.R.E. (deposition date: 1998-10-14, release date: 1999-04-27, Last modification date: 2024-10-23) |
| Primary citation | Uson, I.,Sheldrick, G.M.,de La Fortelle, E.,Bricogne, G.,Di Marco, S.,Priestle, J.P.,Grutter, M.G.,Mittl, P.R. The 1.2 A crystal structure of hirustasin reveals the intrinsic flexibility of a family of highly disulphide-bridged inhibitors. Structure Fold.Des., 7:55-63, 1999 Cited by PubMed Abstract: Leech-derived inhibitors have a prominent role in the development of new antithrombotic drugs, because some of them are able to block the blood coagulation cascade. Hirustasin, a serine protease inhibitor from the leech Hirudo medicinalis, binds specifically to tissue kallikrein and possesses structural similarity with antistasin, a potent factor Xa inhibitor from Haementeria officinalis. Although the 2.4 A structure of the hirustasin-kallikrein complex is known, classical methods such as molecular replacement were not successful in solving the structure of free hirustasin. PubMed: 10368273DOI: 10.1016/S0969-2126(99)80009-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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