3BG8
Crystal structure of Factor XIa in complex with Clavatadine A
Summary for 3BG8
| Entry DOI | 10.2210/pdb3bg8/pdb |
| Descriptor | Coagulation factor XIa light chain, N-(4-carbamimidamidobutyl)ethanamide, BENZAMIDINE, ... (5 entities in total) |
| Functional Keywords | protease inhibitor, factor xia inhibitor complex, covalent inhibitor, alternative splicing, blood coagulation, disease mutation, glycoprotein, heparin-binding, hydrolase, polymorphism, secreted, serine protease |
| Biological source | Homo sapiens (Human) |
| Cellular location | Secreted: P03951 |
| Total number of polymer chains | 1 |
| Total formula weight | 27643.22 |
| Authors | |
| Primary citation | Buchanan, M.S.,Carroll, A.R.,Wessling, D.,Jobling, M.,Avery, V.M.,Davis, R.A.,Feng, Y.,Xue, Y.,Oster, L.,Fex, T.,Deinum, J.,Hooper, J.N.,Quinn, R.J. Clavatadine A, a natural product with selective recognition and irreversible inhibition of factor XIa. J.Med.Chem., 51:3583-3587, 2008 Cited by PubMed Abstract: Bioassay-guided fractionation of a CH2Cl2/MeOH extract of the sponge Suberea clavata using the serine protease factor XIa to detect antithrombotic activity led to the isolation of the new marine natural products, clavatadines A and B. Clavatadines A and B inhibited factor XIa with IC50's of 1.3 and 27 microM, respectively. A crystal structure of protein-inhibitor (clavatadine A) complex was obtained and revealed interesting selective binding and irreversible inhibition of factor XIa. The cocrystal structure provides guidance for the design and synthesis of future factor XIa inhibitors as antithrombotic agents. PubMed: 18510371DOI: 10.1021/jm800314b PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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