Molecular dynamics study of HIV-1 protease-substrate complex: Roles of the water molecules at the loop structures of the active site

Journal of the American Chemical Society

Volumn 122, Issue 23, 2000, Pages 5613-5622

  Okimoto, Noriaki ^a,b   Tsukui, Toshiyuki ^b   Kitayama, Kiyo ^b   Hata, Masayuki ^b   Hoshino, Tyuji ^b   Tsuda, Minoru ^b  

^a INST OF PHYS AND CHEMICAL RESEARCH   (Japan)

^b CHIBA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; PROTEINASE; PROTEINASE INHIBITOR; VIRUS RNA; WATER;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INDUCTION; ENZYME INHIBITOR INTERACTION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; HUMAN IMMUNODEFICIENCY VIRUS 1; MOLECULAR DYNAMICS; PROTEIN DEGRADATION; RNA GENE;

EID: 0034647235     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9929178     Document Type: Article

References (40)

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33. Throughout MM minimizations and MD simulations on the structures in Table 1 (structures 3-7). the respective spaces of the deleted crystal water molecules (spaces 0-4) have been confirmed to be unoccupied by other water molecules supplied in the solvent generation.
34. WAT00 also occupied space 0 during the 100-ps MD simulations.
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