1FPC
ACTIVE SITE MIMETIC INHIBITION OF THROMBIN
Summary for 1FPC
| Entry DOI | 10.2210/pdb1fpc/pdb |
| Related PRD ID | PRD_000376 |
| Descriptor | thrombin, Hirudin, amino{[(4S)-4-({[5-(dimethylamino)naphthalen-1-yl]sulfonyl}amino)-5-(4-ethylpiperidin-1-yl)-5-oxopentyl]amino}methaniminium, ... (5 entities in total) |
| Functional Keywords | serine protease-inhibitor complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Hirudo medicinalis (Medicinal leech) More |
| Cellular location | Secreted, extracellular space: P00734 P00734 Secreted: P28504 |
| Total number of polymer chains | 3 |
| Total formula weight | 35914.99 |
| Authors | Tulinsky, A.,Mathews, I.I. (deposition date: 1994-10-16, release date: 1995-02-27, Last modification date: 2024-10-30) |
| Primary citation | Mathews, I.I.,Tulinsky, A. Active-site mimetic inhibition of thrombin. Acta Crystallogr.,Sect.D, 51:550-559, 1995 Cited by PubMed Abstract: The structures of two mimetic inhibitor complexes of human alpha-thrombin have been determined by X-ray crystallography. One mimics a beta-turn with a bicyclic ring system; the other mimics two different active-site binding modes. The beta-turn mimetic is used to approximate a turn found in the conformation of fibrinopeptide A, which is catalytically released by thrombin in the activation of fibrinogen to fibrin. The binding of the second mimetic is a hybrid between normal substrate and the abnormal binding of the potent natural leech inhibitor hirudin. The binding of the beta-turn mimetic is tenuous, because it is like a substrate, while that of the substrate-hirudin hybrid is that of a tenacious inhibitor (which it is). Structurally retrospect modifications for rational design and improvement of both mimetic inhibitors are proposed. PubMed: 15299843DOI: 10.1107/S0907444994013132 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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