1FV9
Crystal structure of human microurokinase in complex with 2-amino-5-hydroxy-benzimidazole
Summary for 1FV9
| Entry DOI | 10.2210/pdb1fv9/pdb |
| Descriptor | UROKINASE, SULFATE ION, 2-AMINO-5-HYDROXY-BENZIMIDAZOLE (3 entities in total) |
| Functional Keywords | plasminogen activation, blood clotting |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P00749 |
| Total number of polymer chains | 1 |
| Total formula weight | 27835.64 |
| Authors | Nienaber, V. (deposition date: 2000-09-19, release date: 2000-10-18, Last modification date: 2024-11-13) |
| Primary citation | Hajduk, P.J.,Boyd, S.,Nettesheim, D.,Nienaber, V.,Severin, J.,Smith, R.,Davidson, D.,Rockway, T.,Fesik, S.W. Identification of novel inhibitors of urokinase via NMR-based screening. J.Med.Chem., 43:3862-3866, 2000 Cited by PubMed Abstract: Using an NMR-based screen, a novel class of urokinase inhibitors were identified that contain a 2-aminobenzimidazole moiety. The inhibitory potency of this family of inhibitors is similar to that of inhibitors containing a guanidine or amidine group. However, unlike previously described guanidino- or amidino-based inhibitors which have pK(a) values greater than 9.0, urokinase inhibitors containing a 2-aminobenzimidazole have pK(a) values of 7.5. Thus, 2-aminobenzimidazoles may have improved pharmacokinetic properties which could increase the bioavailability of inhibitors which contain this moiety. A crystal structure of one of the lead inhibitors, 2-amino-5-hydroxybenzimidazole, complexed with urokinase reveals the electrostatic and hydrophobic interactions that stabilize complex formation and suggests nearby subsites that may be accessed to increase the potency of this new series of urokinase inhibitors. PubMed: 11052791DOI: 10.1021/jm0002228 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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