4.4 Review

Structure and function of HIV-1 integrase

Journal

CURRENT TOPICS IN MEDICINAL CHEMISTRY
Volume 4, Issue 9, Pages 965-977

Publisher

BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/1568026043388547

Keywords

-

Funding

  1. NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [Z01DK036109] Funding Source: NIH RePORTER

Ask authors/readers for more resources

HIV-1 integrase is a multidomain enzyme which is required for the integration of viral DNA into the host genome. it is one of three enzymes of HIV, the others being the Reverse Transcriptase and the Protease. It is an attractive target for therapeutic drug design. The enzyme consists of three domains. The N-terminal domain has a His(2)Cys(2) motif which chelates zinc, the core domain has the catalytic DDE motif which is required for its enzymatic activity, and the C-terminal domain has an SH3-like fold which binds DNA nonspecifically. We review the structures of various integrase fragments, the core domain with inhibitors bound, and propose a model for DNA binding.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available