NMR-based solution structure of the complex of Lactobacillus casei dihydrofolate reductase with trimethoprim and NADPH [1]

Journal of Biomolecular NMR

Volumn 24, Issue 1, 2002, Pages 67-70

  Polshakov, Vladimir I ^a,b   Smirnov, Eugeni G ^b   Birdsall, Berry ^a   Kelly, Geoff ^a   Feeney, James ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^b Center for Drug Chemistry   (Russian Federation)

Author keywords

Co operative binding; Dihydrofolate reductase; Protein structure; Protein ligand interactions; Trimethoprim

Indexed keywords

BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRIMETHOPRIM; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DRUG BINDING; DRUG BINDING SITE; ENZYME STRUCTURE; LACTOBACILLUS CASEI; LETTER; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; METABOLISM; METHODOLOGY; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION;

BACTERIA (MICROORGANISMS); LACTOBACILLUS CASEI;

BINDING SITES; LACTOBACILLUS CASEI; MODELS, MOLECULAR; NADP; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; TETRAHYDROFOLATE DEHYDROGENASE; TRIMETHOPRIM;

EID: 0036755893     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020659713373     Document Type: Letter

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