Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching

Biochemistry

Volumn 44, Issue 21, 2005, Pages 7687-7695

  Coleman, Matthew D ^a   Bass, Randal B ^a   Mehan, Ryan S ^a   Falke, Joseph J ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BACTERIAL CHEMOTAXIS; CYTOPLASMIC DOMAINS; GLYCINE;

BACTERIA; CELL MEMBRANES; CYTOLOGY; DIMERS; DISEASES; MUTAGENESIS; STRUCTURAL ANALYSIS;

ENZYMES;

ALANINE; ASPARTIC ACID; CHEA KINASE; CYSTEINE; CYTOPLASMIC RECEPTOR; DIMER; GLYCINE; HELIX LOOP HELIX PROTEIN; PHOSPHOTRANSFERASE; PROTEIN HISTIDINE KINASE;

ADAPTATION; ARTICLE; AUTOPHOSPHORYLATION; CHEMICAL MUTAGENESIS; CHEMOTAXIS; CONFORMATIONAL TRANSITION; CYTOPLASM; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME PHOSPHORYLATION; ENZYME REGULATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; RESIDUE ANALYSIS; SIGNAL TRANSDUCTION;

ADAPTATION, PHYSIOLOGICAL; ALANINE; AMINO ACID SUBSTITUTION; ASPARTIC ACID; BACTERIAL PROTEINS; CHEMOTAXIS; CONSERVED SEQUENCE; CYSTEINE; CYTOPLASM; DISULFIDES; ENZYME ACTIVATION; ESCHERICHIA COLI; GLYCINE; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, AMINO ACID; SALMONELLA TYPHIMURIUM; SIGNAL TRANSDUCTION;

BACTERIA (MICROORGANISMS);

EID: 19644374667     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0501479     Document Type: Article

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