Computer-aided molecular modeling of cathepsin E,a possible endothelin-converting enzyme |
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| Affiliation: | 1. LabMol, Faculty of Pharmacy, Universidade Federal de Goias, Goiânia, GO, 74605-170, Brazil;2. NCBios, Universidade Federal de Goias, Jatai, GO, 74605-170, Brazil;3. Fiocruz Ceará - Fundação Oswaldo Cruz, Fortaleza, CE, Brazil;4. Department of Pharmacology, Physiology and Neuroscience, Rutgers University–New Jersey Medical School, Newark, NJ, 07103, United States;5. Collaborations Pharmaceuticals, Inc., 5616 Hilltop Needmore Road, Fuquay-Varina, NC, 27526, United States;1. Graduate School of Science, Osaka Prefecture University, 1-1 Gakuen-cho, Naka-ku, Sakai, Osaka 599-8531, Japan;2. Next Generation Healthcare Innovation Center, Fujitsu Limited, 17-25, Shinkamata 1-chome, Ota-ku, Tokyo, Tokyo 144-8588, Japan;1. Department of Bioengineering, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan;2. Advanced Analysis Center, National Agriculture and Food Research Organization, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-0856, Japan;3. Nard Institute, Ltd., 5-4-1 Minatojima Minamimachi Chuo-ku, Kobe 650-0047, Japan;4. PeptiDream, Inc., 3-25-23 Tonomachi, Kawasaki-ku, Kawasaki City, Kanagawa 210-0821, Japan;5. Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan;1. Institute of Cardiovascular Science, University College London, London, UK;2. INSERM U1148, CHU X. Bichat, 75877 Paris Cedex 18, France;3. Paediatric Cardiology, Great Ormond Street Hospital, London, UK;4. William Harvey Research Institute, Barts and the London School of Medicine, Queen Mary University of London, London, UK;5. Lung Biotechnology, PBC, Silver Spring, MD, USA |
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| Abstract: | A three-dimensional model of human cathepsin E, a possible endothelin-converting enzyme, is constructed using computer-aided molecular modeling techniques. The structure of porcine pepsin, another aspartic protease, was used as a template. The final structure, after all gaps and deletions were made, was optimized using the AMBER-4 package. A dipeptide (Trp-Val) representing the substrate was docked in the putative active site and the whole structure was optimized after several runs of minimization and dynamics calculations. The result of this modeling study showed that the structure of cathepsin E is similar to that of porcine pepsin and has three disulfide bonds that are conserved in both enzymes. There are two Asp-Thr-Gly sequences at the active site of enzyme. The active site cavity is large enough to accommodate its substrate. |
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