Structure of HIV-1 protease in complex with potent inhibitor KNI-272 determined by high-resolution X-ray and neutron crystallography

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 12, 2009, Pages 4641-4646

  Adachi, Motoyasu ^a   Ohhara, Takashi ^a   Kurihara, Kazuo ^a   Tamada, Taro ^a   Honjo, Eijiro ^a   Okazaki, Nobuo ^a   Arai, Shigeki ^a   Shoyama, Yoshinari ^a   Kimura, Kaname ^b   Matsumura, Hiroyoshi ^c,d,e   Sugiyama, Shigeru ^c,d   Adachi, Hiroaki ^c,d,e   Takano, Kazufumi ^c,d,e   Mori, Yusuke ^c,d,e   Hidaka, Koushi ^f   Kimura, Tooru ^f   Hayashi, Yoshio ^f   Kiso, Yoshiaki ^f   Kuroki, Ryota ^a  

^a JAPAN ATOMIC ENERGY AGENCY   (Japan)

^b KYOWA HAKKO KOGYO CO LTD   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^e 313 Photonics Center Building   (Japan)

^f KYOTO PHARMACEUTICAL UNIVERSITY   (Japan)

Author keywords

Drug target; Neutron diffraction; Reaction mechanism transition state analog

Indexed keywords

ASPARTIC ACID; HUMAN IMMUNODEFICIENCY VIRUS 1 PROTEASE; KYNOSTATIN 272; PROTON; STATINE DERIVATIVE; UNCLASSIFIED DRUG; VIRUS ENZYME; OLIGOPEPTIDE; P16 PROTEASE, HUMAN IMMUNODEFICIENCY VIRUS 1; PROTEINASE; PROTEINASE INHIBITOR; WATER;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME BINDING; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROGEN BOND; NEUTRON DIFFRACTION; NONHUMAN; OPTICAL RESOLUTION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; PROTEIN TERTIARY STRUCTURE; STATIC ELECTRICITY;

HUMAN IMMUNODEFICIENCY VIRUS 1;

BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HIV PROTEASE; HIV PROTEASE INHIBITORS; HYDROGEN BONDING; MODELS, MOLECULAR; NEUTRON DIFFRACTION; OLIGOPEPTIDES; PROTEIN STRUCTURE, TERTIARY; STATIC ELECTRICITY; WATER;

EID: 63849087289     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0809400106     Document Type: Article

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