The structure of full-length LysR-type transcriptional regulators. Modeling of the full-length OxyR transcription factor dimer

Nucleic Acids Research

Volumn 31, Issue 5, 2003, Pages 1444-1454

  Zaim, Jolanta ^a   Kierzek, Andrzej M ^a  

^a INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; LYSINE; RNA POLYMERASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR OXYR; UNCLASSIFIED DRUG;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; COMPUTER PROGRAM; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA BINDING MOTIF; DNA TEMPLATE; ESCHERICHIA COLI; MOLECULAR MODEL; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DNA INTERACTION; PROTEIN FAMILY; PROTEIN STRUCTURE; REVIEW; SEQUENCE ALIGNMENT; SEQUENCE DATABASE; SEQUENCE HOMOLOGY; STATISTICAL SIGNIFICANCE; TRANSCRIPTION REGULATION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; DIMERIZATION; DNA; DNA-BINDING PROTEINS; DNA-DIRECTED RNA POLYMERASES; ESCHERICHIA COLI PROTEINS; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; MUTATION; PROTEIN BINDING; REPRESSOR PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TRANSCRIPTION FACTORS;

ACTINOBACTERIA (CLASS); ESCHERICHIA COLI; NEGIBACTERIA; PROKARYOTA; UNCULTURED ACTINOMYCETE;

EID: 0037336620     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg234     Document Type: Review

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