Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases

Nature Structural Biology

Volumn 10, Issue 3, 2003, Pages 168-174

  Young, Tracy A ^a   Delagoutte, Benedicte ^a   Endrizzi, James A ^a   Falick, Arnold M ^a   Alber, Tom ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE DERIVATIVE; PENICILLIN BINDING PROTEIN; PROTEIN KINASE; PROTEIN KINASE PKNB; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATION; CRYSTAL STRUCTURE; METAZOON; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CARRIER PROTEINS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; EUKARYOTIC CELLS; EXTRACELLULAR MATRIX; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; PENICILLIN-BINDING PROTEINS; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN KINASE C; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION; STRUCTURAL HOMOLOGY, PROTEIN;

ACTINOBACTERIA (CLASS); EUKARYOTA; METAZOA; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; PROKARYOTA; UNCULTURED ACTINOMYCETE;

EID: 0037337317     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb897     Document Type: Article

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