Flexible catalytic site conformations implicated in modulation of HIV-1 protease autoprocessing reactions.

Retrovirology

Volumn 8, Issue , 2011, Pages 79-

  Huang, Liangqun ^a   Li, Yanfei ^b   Chen, Chaoping ^b  

^a Department of Environmental and Radiological Health Sciences   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; P16 PROTEASE, HUMAN IMMUNODEFICIENCY VIRUS 1; P6 GAG PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

AMINO ACID SEQUENCE; ARTICLE; BIOCATALYSIS; CELL LINE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; METABOLISM; MOLECULAR GENETICS; PROTEIN MOTIF; PROTEIN PROCESSING; VIROLOGY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BIOCATALYSIS; CATALYTIC DOMAIN; CELL LINE; GAG GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS; HIV INFECTIONS; HIV PROTEASE; HIV-1; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; SUBSTRATE SPECIFICITY;

EID: 80053605302     PISSN: None     EISSN: 17424690     Source Type: Journal    
DOI: 10.1186/1742-4690-8-79     Document Type: Article

References (0)