Third extracellular loop (EC3)-N terminus interaction is important for seven-transmembrane domain receptor function: Implications for an activation microswitch region

Journal of Biological Chemistry

Volumn 285, Issue 41, 2010, Pages 31472-31483

  Rana, Soumendra ^a   Baranski, Thomas J ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOLOGICAL MEMBRANES; CONFORMATIONS; ENZYME ACTIVITY; SIGNALING;

CHEMOKINE RECEPTOR CXCR4; CONSTITUTIVELY ACTIVES; CYSTEINE RESIDUES; EXTRACELLULAR LOOPS; G PROTEIN ACTIVATION; G PROTEIN COUPLED RECEPTORS; MICROSWITCHES; RECEPTOR ACTIVATION; RECEPTOR SIGNALING; SALT BRIDGES; TRANS-MEMBRANE DOMAINS;

AMINO ACIDS;

ARGININE; CHEMOKINE RECEPTOR CXCR4; COMPLEMENT COMPONENT C5; COMPLEMENT RECEPTOR; CYSTEINE; G PROTEIN COUPLED RECEPTOR; GLUTAMIC ACID; GUANINE NUCLEOTIDE BINDING PROTEIN; MUTANT PROTEIN; PHENYLALANINE; RHODOPSIN; SERINE; STROMAL CELL DERIVED FACTOR 1; C5AR1 PROTEIN, HUMAN; COMPLEMENT COMPONENT C5A RECEPTOR; CXCL12 PROTEIN, HUMAN; CXCR4 PROTEIN, HUMAN;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING ASSAY; CELL STRAIN COS7; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; GENE MUTATION; LIGAND BINDING; MOLECULAR MODEL; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; RECEPTOR BINDING; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; WILD TYPE; YEAST CELL; AMINO ACID SUBSTITUTION; ANIMAL; CHLOROCEBUS AETHIOPS; COS 1 CELL LINE; GENE EXPRESSION; GENETICS; HUMAN; METABOLISM; MUTATION; PROTEIN SECONDARY STRUCTURE; SACCHAROMYCES CEREVISIAE;

AMINO ACID SUBSTITUTION; ANIMALS; CERCOPITHECUS AETHIOPS; CHEMOKINE CXCL12; COS CELLS; GENE EXPRESSION; GTP-BINDING PROTEINS; HUMANS; MUTATION; PROTEIN STRUCTURE, SECONDARY; RECEPTOR, ANAPHYLATOXIN C5A; RECEPTORS, COMPLEMENT; RECEPTORS, CXCR4; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION;

EID: 77957765643     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.129213     Document Type: Article

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