Retroviral integrases and their cousins.

Important note: Information in this article was accurate in 1996. The state of the art may have changed since the publication date.

Retroviral integrases and their cousins.

Curr Opin Struct Biol. 1996 Feb;6(1):76-83. Unique Identifier : AIDSLINE MED/96284114
Rice P; Craigie R; Davies DR; Laboratory of Molecular Biology,National Institute of Diabetes; and Digestive and Kidney Diseases, National Institutes of Health,; Bethesda, MD 20892-0540, USA.

Abstract: The recently determined structures of the catalytic domains of HIV integrase, avian sarcoma virus integrase and the Mu transposase are strikingly similar to each other and also exhibit significant similarity to several nucleases. All these enzymes of cut polynucleotides, leaving 3'OH and 5'PO4 groups. The integrase and transposase also possess a strand-transfer activity that splices DNA. The structural similarities among members of this superfamily of polynucleotidyl transferases suggest that they share a similar mechanism of catalysis.

Keywords: Bacterial Proteins/CHEMISTRY Bacteriophage mu/ENZYMOLOGY/GENETICS Catalysis Comparative Study DNA/METABOLISM DNA Nucleotidyltransferases/*CHEMISTRY/GENETICS/METABOLISM Endodeoxyribonucleases/CHEMISTRY Escherichia coli/ENZYMOLOGY HIV-1/ENZYMOLOGY/GENETICS Models, Molecular *Protein Conformation Retroviridae/*ENZYMOLOGY/GENETICS Retroviridae Proteins/*CHEMISTRY/GENETICS/METABOLISM Ribonuclease H, Calf Thymus/CHEMISTRY Sequence Homology, Amino Acid Thermus thermophilus/ENZYMOLOGY JOURNAL ARTICLE REVIEW REVIEW, TUTORIAL
961130
M96B1851

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