Possible role of some groups in the structure and function of HIV-1 protease as revealed by molecular modeling studies

Possible role of some groups in the structure and function of HIV-1 protease as revealed by molecular modeling studies

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...

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Bibliographic Details
Published in:FEBS letters Vol. 247; no. 1; pp. 118 - 122
Main Authors: Pechik, I.V., Gustchina, A.E., Andreeva, N.S., Fedorov, A.A.
Format: Journal Article
Language:English
Published: England Elsevier B.V 10-04-1989
Subjects:
AIDS/HIV
Amino Acid Sequence
Aspartic Acid Endopeptidases
Binding Sites
Endopeptidases
HIV-1
HIV-1 - enzymology
Hydrogen Bonding
Models, Molecular
Molecular Sequence Data
Protein Conformation
proteinase
Retroviral protease
Structure-Activity Relationship
Three-dimensional structure
HIV-1
Retroviral protease
Three-dimensional structure
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Summary: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.
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ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)81252-9