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HIV/AIDS

Findings from National Cancer Institute broaden understanding of HIV/AIDS

Published in AIDS Weekly, January 19th, 2009

According to recent research from the United States, "The crystal structure of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) bound to an RNA/DNA hybrid reveals an extensive network of contacts with the phosphate backbone of the DNA strand similar to 4-9 bp downstream from the ribonuclease H (RNase H) catalytic center. Collectively designated as 'the RNase H primer grip', this motif contains a phosphate binding pocket analogous to the human and Bacillus halodurans RNases H. The notion that the RNase H primer grip mediates the trajectory of RNA/DNA hybrids accessing the RNase H active site suggests that locally neutralizing the phosphate backbone may be exploited to...

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