TAILIEUCHUNG - Báo cáo khoa hoc : Structural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus protease

Interactions between the protease (PR) encoded by the xenotropic murine leukemia virus-related virus and a number of potential inhibitors have been investigated by biochemical and structural techniques. | IFEBS Journal Structural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus protease Mi Li1 2 Alla Gustchina1 Krisztina Matuz3 Jozsef Tozser3 Sirilak Namwong4 Nathan E. Goldfarb5 Ben M. Dunn5 and Alexander Wlodawer1 1 Protein Structure Section Macromolecular Crystallography Laboratory NationalCancer Institute Frederick MD USA 2 Basic Research Program SAIC-Frederick MD USA 3 Department of Biochemistry and Molecular Biology Faculty of Medicine University of Debrecen Hungary 4 Department of Biotechnology Faculty of Science and Technology Suan Sunandha Rajabhat University Bangkok Thailand 5 Department of Biochemistry and Molecular Biology University of Florida Gainesville USA Keywords aspartic protease enzyme inhibition inhibitor binding retrovirus Correspondence A. Wlodawer NationalCancer Institute MCL Bldg 536 Rm 5 Frederick MD 21702-1201 USA Fax 1 301 846 6322 Tel 1 301 846 5036 E-mail wlodawer@ Received 5 August 2011 revised 15 September 2011 accepted 21 September 2011 doi Interactions between the protease PR encoded by the xenotropic murine leukemia virus-related virus and a number of potential inhibitors have been investigated by biochemical and structural techniques. It was observed that several inhibitors used clinically against HIV PR exhibit nanomolar or even subnanomolar values of Ki depending on the exact experimental conditions. Both TL-3 a universal inhibitor of retroviral PRs and some inhibitors originally shown to inhibit plasmepsins were also quite potent whereas inhibition by pepstatin A was considerably weaker. Crystal structures of the complexes of xenotropic murine leukemia virus-related virus PR with TL-3 amprenavir and pepstatin A were solved at high resolution and compared with the structures of complexes of these inhibitors with other retropepsins. Whereas TL-3 and amprenavir bound in a predictable manner spanning the substrate-binding site of the

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