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Possible role of some groups in the structure and function of HIV‐1 protease as revealed by molecular modeling studies
Author(s) -
Pechik I.V.,
Gustchina A.E.,
Andreeva N.S.,
Fedorov A.A.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81252-9
Subject(s) - protease , proteases , rous sarcoma virus , enzyme , chemistry , monomer , human immunodeficiency virus (hiv) , structure function , molecular model , biochemistry , biology , stereochemistry , virology , gene , organic chemistry , physics , polymer , particle physics
Retroviral proteases belong to the class of aspartic proteases. A molecular model of HIV‐1 protease has been built on the basis of the consensus template specific for the domains of these enzymes. The template region comprises more than a half of the HIV‐1 protease monomer structure, it includes the active site, formed at the junction of the two monomers, binding pockets of the enzyme, and some other molecular segments. These regions can be more conveniently described than other parts of the structure. Some properties of the HIV‐1 protease molecule are discussed, as well as of probable inhibitors. The properties of the model structure are in good agreement with the recent results of crystallographic studies of Rous sarcoma virus protease.