Structure of a G48H mutant of HIV-1 protease explains how glycine-48 replacements produce mutants resistant to inhibitor drugs

FEBS Letters

Volumn 420, Issue 1, 1997, Pages 11-16

  Hong, Lin ^a   Zhang, Xue Jun ^a   Foundling, Steve ^a   Hartsuck, Jean Ann ^a,b   Tang, Jordan ^a,b  

^a OKLAHOMA MEDICAL RESEARCH FOUNDATION   (United States)

^b UNIVERSITY OF OKLAHOMA COLLEGE OF MEDICINE   (United States)

Author keywords

Drug resistance; HIV protease; Mutation; Saquinavir

Indexed keywords

PROTEASOME; PROTEINASE; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; SAQUINAVIR; U 89360E; UNCLASSIFIED DRUG; VIRUS ENZYME;

ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DRUG RESISTANCE; ENZYME ACTIVITY; ENZYME INHIBITION; HUMAN IMMUNODEFICIENCY VIRUS 1; IN VITRO STUDY; MODEL; MUTANT; PRIORITY JOURNAL;

DRUG RESISTANCE, MICROBIAL; GLYCINE; HIV PROTEASE; HIV PROTEASE INHIBITORS; HIV-1; HUMANS; MODELS, MOLECULAR; MUTATION; OLIGOPEPTIDES; SAQUINAVIR;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; RNA VIRUSES;

EID: 0031583997     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)01477-4     Document Type: Article

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