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PMID: 2278102 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

The 3-D structure of HIV-1 proteinase and the design of antiviral agents for the treatment of AIDS.

Trends in biochemical sciences ·Vol. 15 ·No. 11 ·1990-11-00 ·Pages 425-30

Blundell TL, Lapatto R, Wilderspin AF, Hemmings AM, Hobart PM, Danley DE, Whittle PJ

Abstract

A proteinase is essential for replication of HIV. Cloning and chemical synthesis have provided a sufficient supply of HIV-1 proteinase for the determination of its three-dimensional structure. Analogies between the structures of HIV-1 proteinase and the mammalian enzyme renin, which is involved in the control of blood pressure, have given important clues concerning the design of specific inhibitors that have antiviral activity.

MeSH Terms

Acquired Immunodeficiency Syndrome/drug therapy Amino Acid Sequence Animals Antiviral Agents/chemistry,therapeutic use Drug Design HIV Protease/chemistry,genetics Humans Molecular Sequence Data Pepsin A/genetics Protease Inhibitors/chemistry,therapeutic use Protein Conformation

Chemicals

Antiviral Agents Protease Inhibitors HIV Protease Pepsin A

Authors & Affiliations

7 authors, click to expand affiliations / ORCID

Blundell T L

Department of Crystallography, Birkbeck College, London, UK.

Lapatto R

Wilderspin A F

Hemmings A M

Hobart P M

Danley D E

Whittle P J

Article Info

Journal

Trends in biochemical sciences

Abbr.

Trends Biochem Sci

ISSN

0968-0004

DOI

10.1016/0968-0004(90)90280-o

Published

1990-11-00

Pages

425-30

Language

English

Region

England

NLM ID

7610674

Subset

External Links

PubMed source DOI: 10.1016/0968-0004(90)90280-o View journal details

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The 3-D structure of HIV-1 proteinase and the design of antiviral agents for the treatment of AIDS.

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