1ANT
BIOLOGICAL IMPLICATIONS OF A 3 ANGSTROMS STRUCTURE OF DIMERIC ANTITHROMBIN
Summary for 1ANT
Entry DOI | 10.2210/pdb1ant/pdb |
Descriptor | ANTITHROMBIN (1 entity in total) |
Functional Keywords | serine protease inhibitor |
Biological source | Homo sapiens (human) |
Cellular location | Secreted, extracellular space: P01008 |
Total number of polymer chains | 2 |
Total formula weight | 98202.03 |
Authors | Carrell, R.W.,Stein, P.E.,Fermi, G.,Wardell, M.R. (deposition date: 1994-02-28, release date: 1995-01-26, Last modification date: 2024-10-23) |
Primary citation | Carrell, R.W.,Stein, P.E.,Fermi, G.,Wardell, M.R. Biological implications of a 3 A structure of dimeric antithrombin. Structure, 2:257-270, 1994 Cited by PubMed Abstract: Antithrombin, a member of the serpin family of inhibitors, controls coagulation in human plasma by forming complexes with thrombin and other coagulation proteases in a process greatly accelerated by heparin. The structures of several serpins have been determined but not in their active conformations. We have determined the structure of intact antithrombin in order to study its mechanism of activation, particularly with respect to heparin, and the dysfunctions of this mechanism that predispose individuals to thrombotic disease. PubMed: 8087553DOI: 10.1016/S0969-2126(00)00028-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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