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Publication Abstract from PubMed

Integrase plays a critical role in the recombination of viral DNA into the host genome. Therefore, over the past decade, it has been a hot target of drug design in the fight against type 1 human immunodeficiency virus (HIV-1). Bovine immunodeficiency virus (BIV) integrase has the same function as HIV-1 integrase. We have determined crystal structures of the BIV integrase catalytic core domain (CCD) in two different crystal forms at a resolution of 2.45 A and 2.2 A, respectively. In crystal form I, BIV integrase CCD forms a back-to-back dimer, in which the two active sites are on opposite sides. This has also been seen in many of the CCD structures of HIV-1 integrase that were determined previously. However, in crystal form II, BIV integrase CCD forms a novel face-to-face dimer in which the two active sites are close to each other. Strikingly, the distance separating the two active sites is approximately 20 A, a distance that perfectly matches a 5-base pair interval. Based on these data, we propose a model for the interaction of integrase with its target DNA, which is also supported by many published biochemical data. Our results provide important clues for designing new inhibitors against HIV-1.

Crystal structures of catalytic core domain of BIV integrase: implications for the interaction between integrase and target DNA.,Yao X, Fang S, Qiao W, Geng Y, Shen Y Protein Cell. 2010 Apr;1(4):363-70. Epub 2010 May 8. PMID:21203948^[1]

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