The apo-structure of the low molecular weight protein-tyrosine phosphatase A (MptpA) from Mycobacterium tuberculosis allows for better target-specific drug development

Journal of Biological Chemistry

Volumn 287, Issue 41, 2012, Pages 34569-34582

  Stehle, Tanja ^a   Sreeramulu, Sridhar ^a   Löhr, Frank ^a   Richter, Christian ^a   Saxena, Krishna ^a   Jonker, Hendrik R A ^a   Schwalbe, Harald ^a  

^a GOETHE UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACIDS; BINDING INTERFACE; CELLULAR PROCESS; DRUG DEVELOPMENT; FREEFORMS; HIGH MOLECULAR WEIGHT; HIGH RESOLUTION; HUMAN DISEASE; LIGAND BINDING; LIGAND-FREE STRUCTURES; LOW MOLECULAR WEIGHT; MYCOBACTERIUM TUBERCULOSIS; OPEN CONFORMATION; PATHOGENIC BACTERIUM; PHOSPHATE BINDING; PHOSPHATE IONS; PROTEIN-TYROSINE KINASE; PROTEIN-TYROSINE PHOSPHATASE; SEQUENCE SIMILARITY; SOLUTION NMR; TYROSINE RESIDUES; VIRULENCE FACTORS;

LIGANDS; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHATASES; PHOSPHORYLATION; PROTEINS; TUBES (COMPONENTS);

AMINO ACIDS;

PHOSPHATE; PROTEIN TYROSINE KINASE A; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE A; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CATALYSIS; COMPETITIVE INHIBITION; CONTROLLED STUDY; DRUG TARGETING; ENZYME ACTIVITY; HYDROGEN BOND; MASS SPECTROMETRY; MOLECULAR WEIGHT; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

APOENZYMES; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; CYCLIC AMP-DEPENDENT PROTEIN KINASES; DRUG DELIVERY SYSTEMS; HUMANS; MACROPHAGES; MYCOBACTERIUM TUBERCULOSIS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHORYLATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN TYROSINE PHOSPHATASES;

EID: 84867280562     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.399261     Document Type: Article

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