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 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.
Pechik
I V
IV
V.A. Engelhardt Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow.
Gustchina
A E
AE
Andreeva
N S
NS
Fedorov
A A
AA
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases; D001665:Binding Sites; D010450:Endopeptidases; D015497:HIV-1 / Q000201:enzymology*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases