HIV/AIDS

Study findings from Case Western Reserve University, Medical Department broaden understanding of HIV/AIDS

Published in AIDS Weekly, October 12th, 2009

According to recent research published in the journal Biochemistry, "Crystal structures and simulations suggest that conformational changes are-critical for the function of HIV-1 reverse transcriptase. The enzyme is an asymmetric heterodimer of two subunits, p66 and p51."

"The two subunits have the same N-terminal sequence, With the p51 subunit lacking the C-terminal RNase I-I domain. We used hydrogen exchange mass spectrometry to probe the structural dynamics of RT. H/D exchange revealed that the fingers and palm subdomains of both subunits form the stable core of the heterodimer, In the crystal structure, the tertiary fold of the p51 subunit is more compact...

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Source: AIDS Weekly (2009-10-12)

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