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Broggio, D.*; Bento, J.*; Caldeira, M.*; Cardenas-Mendez, E.*; Farah, J.*; Fonseca, T.*; Konvalinka, C.*; Liu, L.*; Perez, B.*; Capello, K.*; et al.
Radiation Measurements, 47(7), p.492 - 500, 2012/07
Times Cited Count:23 Percentile:83.88(Nuclear Science & Technology)Adachi, Motoyasu; Tamada, Taro; Hidaka, Koshi*; Hayashi, Yoshio*; Freire, E.*; Kiso, Yoshiaki*; Kuroki, Ryota
no journal, ,
The development of HIV protease (HIVPR) inhibitors is regarded as a major success of structure-based drug design, and the inhibitors of HIVPR are important compounds to establish highly active antiretroviral therapy for AIDS. Adverse effects linked to the use of HIVPR inhibitors, and the emergence of HIV mutants resistant to current drugs, remain critical factors in the clinical failure of antiviral therapy. We are currently working on structure analysis of HIVPR inhibitor complex using both ultra-high resolution X-ray and neutron crystallography. To obtain the HIVPR, the gene of HIVPR was expressed in E. coli and successfully refolded. A crystal of HIVPR with KNI-272 was obtained. This crystal diffracted X-ray beyond 1.1 angstroms resolution, which is much higher than the previous structure. Refinement using anisotropic temperature factors has produced more detailed structure and dynamic information about the HIVPR inhibitor complex, including details of bound water molecules.