Frontiers in Medicinal Chemistry

Volume: 3

Indexed in: Scopus, EMBASE, Chemical Abstracts, EBSCO, Ulrich's Periodicals Directory.

Frontiers in Medicinal Chemistry is a book series devoted to the review of areas of important topical interest to medicinal chemists and others in allied disciplines. Frontiers in Medicinal Chemistry ...
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Structure and Function of HIV-1 Integrase: An Update

Pp. 3-22 (20)

Thang K. Chiu and David R. Davies

Abstract

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 Reverse Transcriptase and Protease. It is an attractive target for therapeutic drug design. The enzyme consists of three domains. The N-terminal domain has a His2Cys2 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.

Affiliation:

NIH, NIDDK, Laboratory of Molecular Biology, Building 5, Room 338, Bethesda, MD 20892-0560, USA.