1B3K
Plasminogen activator inhibitor-1
Summary for 1B3K
| Entry DOI | 10.2210/pdb1b3k/pdb |
| Related | 1C5G |
| Descriptor | PLASMINOGEN ACTIVATOR INHIBITOR-1 (1 entity in total) |
| Functional Keywords | serpin, pai-1, inhibitor, blood clotting |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P05121 |
| Total number of polymer chains | 4 |
| Total formula weight | 171128.09 |
| Authors | Sharp, A.M.,Stein, P.E.,Pannu, N.S.,Read, R.J. (deposition date: 1998-12-11, release date: 1999-12-11, Last modification date: 2024-04-03) |
| Primary citation | Sharp, A.M.,Stein, P.E.,Pannu, N.S.,Carrell, R.W.,Berkenpas, M.B.,Ginsburg, D.,Lawrence, D.A.,Read, R.J. The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure Fold.Des., 7:111-118, 1999 Cited by PubMed Abstract: Plasminogen activator inhibitor 1 (PAI-1) is a serpin that has a key role in the control of fibrinolysis through proteinase inhibition. PAI-1 also has a role in regulating cell adhesion processes relevant to tissue remodeling and metastasis; this role is mediated by its binding to the adhesive glycoprotein vitronectin rather than by proteinase inhibition. Active PAI-1 is metastable and spontaneously transforms to an inactive latent conformation. Previous attempts to crystallize the active conformation of PAI-1 have failed. PubMed: 10368279DOI: 10.1016/S0969-2126(99)80018-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.99 Å) |
Structure validation
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