A team from Imperial College London and Harvard University report solving the 3-D crystal structure of a retroviral integrase enzyme bound with viral DNA. The work is published in Nature in a paper titled “Retroviral intasome assembly and inhibition of DNA strand transfer.”
Integrase is an essential retroviral enzyme that binds both termini of linear viral DNA and inserts them into a host cell chromosome, explains lead author, Peter Cherepanov, Ph.D., and colleagues. However, to date, the structure of full-length retroviral integrase, either separately or in complex with DNA, has been lacking. Moreover, the researchers add, while clinically useful inhibitors of HIV integrase have been developed, their mechanism of action remains speculative. The structural organization of the enzyme active site, which is believed to adopt its functional state only after viral DNA binding, is also unknown.
http://www.genengnews.com/news/bnitem.aspx?name=74423430&source=genwire
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