Biased Gs versus Gq proteins and β-arrestin signaling in the NK1 receptor determined by interactions in the water hydrogen bond network

Journal of Biological Chemistry

Volumn 290, Issue 40, 2015, Pages 24495-24508

  Valentin Hansen, Louise ^a,b   Frimurer, Thomas M ^c   Mokrosinski, Jacek ^a,b   Holliday, Nicholas D ^d   Schwartz, Thue W ^a,b  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b Capital Region   (Denmark)

^c University of Copenhagen   (Denmark)

^d UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CHEMICAL ACTIVATION; MOLECULAR DYNAMICS; SIGNAL TRANSDUCTION;

HYDROGEN BOND NETWORKS; MOLECULAR DYNAMICS SIMULATIONS; MUTATIONAL ANALYSIS; MUTATIONAL CHANGES; RECEPTOR SIGNALS; SIGNAL TRANSDUCTION PATHWAYS; SIGNALING PATHWAYS; TRANSMEMBRANE RECEPTORS;

HYDROGEN BONDS;

ALANINE; BETA ARRESTIN; CARBOXYLIC ACID; GHRELIN RECEPTOR; NEUROKININ 1 RECEPTOR; SODIUM ION; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; RETINA S ANTIGEN; SODIUM; STIMULATORY GUANINE NUCLEOTIDE BINDING PROTEIN; WATER;

ALLOSTERISM; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING AFFINITY; HUMAN; HYDROGEN BOND; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; ANIMAL; BINDING SITE; CHEMISTRY; CHLOROCEBUS AETHIOPS; COS CELL LINE; DNA MUTATIONAL ANALYSIS; GENETIC TRANSFECTION; METABOLISM; MOLECULAR DYNAMICS; MONTE CARLO METHOD; PROTEIN CONFORMATION; SIGNAL TRANSDUCTION; X RAY CRYSTALLOGRAPHY;

ALANINE; ALLOSTERIC SITE; ANIMALS; ARRESTINS; BETA-ARRESTINS; CERCOPITHECUS AETHIOPS; COS CELLS; CRYSTALLOGRAPHY, X-RAY; DNA MUTATIONAL ANALYSIS; GTP-BINDING PROTEIN ALPHA SUBUNITS, GQ-G11; GTP-BINDING PROTEIN ALPHA SUBUNITS, GS; HUMANS; HYDROGEN BONDING; MOLECULAR DYNAMICS SIMULATION; MONTE CARLO METHOD; PROTEIN CONFORMATION; RECEPTORS, G-PROTEIN-COUPLED; RECEPTORS, GHRELIN; RECEPTORS, NEUROKININ-1; SIGNAL TRANSDUCTION; SODIUM; TRANSFECTION; WATER;

EID: 84943329391     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.m115.641944     Document Type: Article

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