Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1.

Article Details

Citation

Navia MA, Fitzgerald PM, McKeever BM, Leu CT, Heimbach JC, Herber WK, Sigal IS, Darke PL, Springer JP

Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1.

Nature. 1989 Feb 16;337(6208):615-20.

PubMed ID
2645523 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Gag-Pol polyproteinP12497Details