TAILIEUCHUNG - Báo cáo khoa học: Piecing together the structure of retroviral integrase, an important target in AIDS therapy

Integrase (IN) is one of only three enzymes encoded in the genomes of all retroviruses, and is the one least characterized in structural terms. IN cata-lyzes processing of the ends of a DNA copy of the retroviral genome and its concerted insertion into the chromosome of the host cell. | ễFEBS Journal REVIEW ARTICLE Piecing together the structure of retroviral integrase an important target in AIDS therapy Mariusz Jaskolski1 2 Jerry N. Alexandratos3 Grzegorz Bujacz2 4 and Alexander Wlodawer3 1 Department of Crystallography Faculty of Chemistry A. Mickiewicz University Poznan Poland 2 Center for Biocrystallographic Research Institute of Bioorganic Chemistry Polish Academy of Sciences Poznan Poland 3 Macromolecular Crystallography Laboratory NationalCancer Institute at Frederick MD USA 4 Institute of TechnicalBiochemistry TechnicalUniversity of Lodz Poland Keywords AIDS antiretroviral drugs DNA integration HIV integrase Correspondence A. Wlodawer Macromolecular Crystallography Laboratory NationalCancer Institute at Frederick Frederick MD 21702 USA Fax 1 301 846 6322 Tel 1 301 846 5036 E-mail wlodawer@ Note This review is dedicated to David Eisenberg on the occasion of his 70th birthday. Received 13 January 2009 revised 17 February 2009 accepted 17 March 2009 doi Integrase IN is one of only three enzymes encoded in the genomes of all retroviruses and is the one least characterized in structural terms. IN catalyzes processing of the ends of a DNA copy of the retroviral genome and its concerted insertion into the chromosome of the host cell. The protein consists of three domains the central catalytic core domain flanked by the N-terminal and C-terminal domains the latter being involved in DNA binding. Although the Protein Data Bank contains a number of NMR structures of the N-terminal and C-terminal domains of HIV-1 and HIV-2 simian immunodeficiency virus and avian sarcoma virus IN as well as X-ray structures of the core domain of HIV-1 avian sarcoma virus and foamy virus IN plus several models of two-domain constructs no structure of the complete molecule of retroviral IN has been solved to date. Although no experimental structures of IN complexed with the DNA substrates are at hand the catalytic mechanism of IN .

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