Mycobacterium tuberculosis dihydrofolate reductase reveals two conformational states and a possible low affinity mechanism to antifolate drugs

Structure

Volumn 22, Issue 1, 2014, Pages 94-103

  Dias, Marcio Vinicius Bertacine ^a,b   Tyrakis, Petros ^a   Domingues, Romenia Ramos ^b   Leme, Adriana Franco Paes ^b   Blundell, Tom L ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b BRAZILIAN CENTER FOR RESEARCH IN ENERGY AND MATERIALS CNPEM   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOGUANIL; DIHYDROFOLATE REDUCTASE; NICOTINAMIDE; PYRIMETHAMINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TETRAHYDROFOLIC ACID; TRIMETHOPRIM; FOLIC ACID ANTAGONIST;

ARTICLE; BINDING AFFINITY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME STRUCTURE; HYDROGEN BOND; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR WEIGHT; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; CALORIMETRY; CHEMICAL STRUCTURE; CONFORMATIONAL TRANSITION; PROTEIN STRUCTURE;

MYCOBACTERIUM TUBERCULOSIS;

BACTERIAL PROTEINS; CALORIMETRY; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; ESCHERICHIA COLI; FOLIC ACID ANTAGONISTS; LIGANDS; MOLECULAR DOCKING SIMULATION; MUTAGENESIS, SITE-DIRECTED; MYCOBACTERIUM TUBERCULOSIS; PROGUANIL; PROTEIN CONFORMATION; PYRIMETHAMINE; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TETRAHYDROFOLATE DEHYDROGENASE; THERMODYNAMICS; TRIAZINES; TRIMETHOPRIM;

EID: 84891875929     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.09.022     Document Type: Article

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