3V7T
Crystal Structure of Human Beta-Tryptase Complexed with a Synthetic Inhibitor with a Tropanylamide Scaffold
Summary for 3V7T
| Entry DOI | 10.2210/pdb3v7t/pdb |
| Descriptor | TPSB2 protein, {(3-exo)-3-[5-(aminomethyl)-2-fluorophenyl]-8-azabicyclo[3.2.1]oct-8-yl}(4-bromo-3-methyl-5-propoxythiophen-2-yl)methanone, CARBONATE ION, ... (4 entities in total) |
| Functional Keywords | tryptase, serine protease, tetramer, protein-ligand complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 112067.51 |
| Authors | Zhang, Y.,Colonna, C.,Michot, N. (deposition date: 2011-12-22, release date: 2012-03-14, Last modification date: 2017-11-08) |
| Primary citation | Liang, G.,Choi-Sledeski, Y.M.,Shum, P.,Chen, X.,Poli, G.B.,Kumar, V.,Minnich, A.,Wang, Q.,Tsay, J.,Sides, K.,Kang, J.,Zhang, Y. A beta-tryptase inhibitor with a tropanylamide scaffold to improve in vitro stability and to lower hERG channel binding affinity Bioorg.Med.Chem.Lett., 22:1606-1610, 2012 Cited by PubMed Abstract: Tropanylamide was investigated as a possible scaffold for β-tryptase inhibitors with a basic benzylamine P1 group and a substituted thiophene P4 group. Comparing to piperidinylamide, the tropanylamide scaffold is much more rigid, which presents less opportunity for the inhibitor to bind with off-target proteins, such as cytochrome P450, SSAO, and hERG potassium channel. The proposed binding mode was further confirmed by an in-house X-ray structure through co-crystallization. PubMed: 22264487DOI: 10.1016/j.bmcl.2011.12.127 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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