Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1.
The crystal structure of the protease of the human immunodeficiency virus type (HIV-1), which releases structural proteins and enzymes from viral polyprotein products, has been determined to 3 A resolution. Large regions of the protease dimer, including the active site, have structural homology to the family of microbial aspartyl proteases. The structure suggests a mechanism for the autoproteolytic release of protease and a role in the control of virus maturation.
Navia
M A
MA
Department of Biophysical Chemistry, Merck Sharp and Dohme Research Laboratories, Rahway, New Jersey 07065.
Fitzgerald
P M
PM
McKeever
B M
BM
Leu
C T
CT
Heimbach
J C
JC
Herber
W K
WK
Sigal
I S
IS
Darke
P L
PL
Springer
J P
JP
D016282:Aspartic Acid Endopeptidases; D010450:Endopeptidases / Q000378:metabolism*; D015497:HIV-1 / Q000201:enzymology*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation
D046911:Macromolecular Substances; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases