Three-dimensional Structure of Aspartyl Protease from Human Immunodeficiency Virus HIV-1

Overview

Journal Nature

Specialty Science

Date 1989 Feb 16

PMID 2645523

Citations 179

Authors

M A Navia

P M Fitzgerald

B M McKeever

C T Leu

J C Heimbach

W K Herber

I S Sigal

P L Darke

J P Springer

Affiliations

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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.

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