How conformational changes can affect catalysis, inhibition and drug resistance of enzymes with induced-fit binding mechanism such as the HIV-1 protease

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 5, 2013, Pages 867-873

  Weikl, Thomas R ^a   Hemmateenejad, Bahram ^a,b  

^a MAX PLANCK INSTITUTE OF COLLOIDS AND INTERFACES   (Germany)

^b SHIRAZ UNIVERSITY   (Iran)

Author keywords

Conformational selection; Enzyme dynamics; HIV 1 protease; Induced fit; Multi drug resistance; Non active site mutation

Indexed keywords

AMPRENAVIR; DARUNAVIR; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE; INDINAVIR; LOPINAVIR; NELFINAVIR; RITONAVIR; SAQUINAVIR;

ARTICLE; CATALYSIS; CHEMICAL REACTION; COMPARATIVE STUDY; CONFORMATIONAL TRANSITION; DRUG RESISTANCE; ENZYME CONFORMATION; ENZYME INHIBITION; EQUILIBRIUM CONSTANT; MOLECULE; PRIORITY JOURNAL; PROTEIN EXPRESSION; WILD TYPE;

BIOCATALYSIS; CATALYTIC DOMAIN; DRUG RESISTANCE, VIRAL; HIV PROTEASE; HIV-1; MUTATION; PROTEIN CONFORMATION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84876296670     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.01.027     Document Type: Article

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