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Volumn 23, Issue 5, 2013, Pages 1279-1284
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Structural analysis of the active sites of dihydrofolate reductase from two species of Candida uncovers ligand-induced conformational changes shared among species
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Author keywords
Antifolate; DHFR; Molecular dynamics; Protein flexibility; X ray crystallography
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Indexed keywords
DIHYDROFOLATE REDUCTASE;
FOLIC ACID ANTAGONIST;
LIGAND;
PHENYLALANINE;
THREONINE;
ANTIFUNGAL ACTIVITY;
ARTICLE;
CANDIDA;
CANDIDA ALBICANS;
CANDIDA GLABRATA;
CONTROLLED STUDY;
CRYSTAL STRUCTURE;
DRUG POTENCY;
DRUG SELECTIVITY;
DRUG SOLUBILITY;
DRUG SYNTHESIS;
ENZYME ACTIVE SITE;
ENZYME CONFORMATION;
FUNGAL STRAIN;
HUMAN;
IC 50;
MOLECULAR DYNAMICS;
MOLECULAR PROBE;
NONHUMAN;
AMINO ACID SEQUENCE;
CANDIDA;
CATALYTIC DOMAIN;
CRYSTALLOGRAPHY, X-RAY;
HUMANS;
LIGANDS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PROTEIN CONFORMATION;
STRUCTURE-ACTIVITY RELATIONSHIP;
TETRAHYDROFOLATE DEHYDROGENASE;
CANDIDA;
CANDIDA ALBICANS;
CANDIDA GLABRATA;
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EID: 84873707989
PISSN: 0960894X
EISSN: 14643405
Source Type: Journal
DOI: 10.1016/j.bmcl.2013.01.008 Document Type: Article |
Times cited : (16)
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References (14)
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