title: Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1.
abstract: 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.
authors.affiliation: Department of Biophysical Chemistry, Merck Sharp and Dohme Research Laboratories, Rahway, New Jersey 07065.
authors.forename: M A
authors.initials: MA
authors.lastname: Navia
authors.forename: P M
authors.initials: PM
authors.lastname: Fitzgerald
authors.forename: B M
authors.initials: BM
authors.lastname: McKeever
authors.forename: C T
authors.initials: CT
authors.lastname: Leu
authors.forename: J C
authors.initials: JC
authors.lastname: Heimbach
authors.forename: W K
authors.initials: WK
authors.lastname: Herber
authors.forename: I S
authors.initials: IS
authors.lastname: Sigal
authors.forename: P L
authors.initials: PL
authors.lastname: Darke
authors.forename: J P
authors.initials: JP
authors.lastname: Springer
mesh_terms: D016282:Aspartic Acid Endopeptidases; D010450:Endopeptidases / Q000378:metabolism*; D015497:HIV-1 / Q000201:enzymology*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D046911:Macromolecular Substances; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases