Protein modeling of human prorenin using the molecular dynamics method |
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| Institution: | 1. Instituto de Ciencias Marinas de Andalucía (ICMAN-CSIC), Campus Universitario Río San Pedro, 11519 Puerto Real, Cádiz, Spain;2. Departamento de Biomedicina, Biotecnología y Salud Pública, Facultad de Ciencias, Universidad de Cádiz, Campus Universitario Río San Pedro, 11519 Puerto Real, Cádiz, Spain;1. Centre for Marine Sciences, CCMAR-CIMAR Laboratório Associado, Universidade do Algarve, Campus do Gambelas, 8005-139, Faro, Portugal;2. The Roslin Institute and R(D)SVS, University of Edinburgh, The Roslin Building, Easter Bush, Midlothian, EH25 9RG, United Kingdom;3. MPI Molecular Genetics, Ihnestrasse 63-73, D-14195 Berlin-Dahlem, Germany;4. Max-Planck-Institut für Pflanzenzüchtungsforschung Carl-von-Linné-Weg 10, D-50829 Köln, Germany;5. Laboratory of Applied Fish Genetics and Fish Breeding, Department of Aquaculture and Fisheries Management, Technological Educational Institute of Messolonghi, Nea Ktiria, 30200 Messolonghi, Greece;6. Laboratory of Biodiversity and Evolutionary Genomics, University of Leuven, Ch. Deberiotstraat 32, B-3000 Leuven, Belgium;1. School of Physical Education, Xi''an Technological University, Xi''an, Shaanxi Province, China;2. Department of Gynecology, Chengyang People''s Hospital, Qingdao, Shandong Province, China;3. Department of Neurology, Chengyang People''s Hospital, Qingdao, Shandong Province, China;4. Department of Gastroenterology, The Third People''s Hospital of Datong, Datong, Shanxi Province, China;5. Department of General Urgery, Yuquan Hospital of Tsinghua University, Beijing, China |
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| Abstract: | To study the activation-inactivation mechanism of the renin zymogen, prorenin, a tertiary structural model of human prorenin was constructed using computer graphics and molecular dynamics calculations, based on the pepsinogen structure. This prorenin model shows that the folded prosegment polypeptide can fit into the substrate binding cleft of the renin moiety. The three positively charged residues, Arg 10, Arg 15, and Arg 20, in the prosegment make salt bridges with Asp 225, Glu 331, and Asp 60, respectively, in renin. Arg 43, which is in the processing site, forms salt bridges with the catalytic residues of Asp 81 and Asp 269. These ionic interactions between the prosegment and the renin may contribute to keeping the prorenin structure as an inactive form. |
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