Structural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus protease.
Structural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus protease.
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DOI：
10.1111/j.1742-4658.2011.08364.x
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发表时间：
2011-11
期刊：
影响因子：
--
通讯作者：
Wlodawer A
中科院分区：
文献类型：
--
作者：
Li M;Gustchina A;Matúz K;Tözsér J;Namwong S;Goldfarb NE;Dunn BM;Wlodawer A
Interactions between the protease (PR) encoded by the xenotropic murine leukemia virus-related virus (XMRV) 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 exact experimental conditions. TL-3, a universal inhibitor of retroviral proteases, as well as 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 XMRV PR with TL-3, amprenavir, and pepstatin A were solved at high resolution and compared to the structures of these inhibitors complexed with other retropepsins. Whereas TL-3 and amprenavir bind in a predictable manner spanning the substrate-binding site of the enzyme, two molecules of pepstatin A bind simultaneously in an unprecedented manner, leaving the catalytic water molecule in place.
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影响因子：
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