3l3u

Publication Abstract from PubMed

HIV integrase (IN) is an essential enzyme in HIV replication and an important target for drug design. IN has been shown to interact with a number of cellular and viral proteins during the integration process. Disruption of these important interactions could provide a mechanism for allosteric inhibition of IN. We present the highest resolution crystal structure of the IN core domain to date. We also present a crystal structure of the IN core domain in complex with sucrose which is bound at the dimer interface in a region that has previously been reported to bind integrase inhibitors.

Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site.,Wielens J, Headey SJ, Jeevarajah D, Rhodes DI, Deadman J, Chalmers DK, Scanlon MJ, Parker MW FEBS Lett. 2010 Apr 16;584(8):1455-62. Epub 2010 Mar 16. PMID:20227411^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.