ELIC-α7 nicotinic acetylcholine receptor (α7nAChR) chimeras reveal a prominent role of the extracellular-transmembrane domain interface in allosteric modulation

Journal of Biological Chemistry

Volumn 289, Issue 20, 2014, Pages 13851-13857

  Tillman, Tommy S ^a   Seyoum, Edom ^a   Mowrey, David D ^a   Xu, Yan ^a   Tang, Pei ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CHEMICAL ACTIVATION;

ALLOSTERIC MODULATION; EXTRACELLULAR DOMAINS; HIGH-RESOLUTION STRUCTURES; LIGAND-GATED ION CHANNELS; NICOTINIC ACETYLCHOLINE RECEPTORS; POSITIVE ALLOSTERIC MODULATOR; STRINGENT REQUIREMENT; SYNAPTIC TRANSMISSION;

MODULATION;

BUNGAROTOXIN RECEPTOR; HYBRID PROTEIN;

ALLOSTERISM; AMINO ACID SEQUENCE; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; EXTRACELLULAR SPACE; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN ENGINEERING; PROTEIN TERTIARY STRUCTURE;

ALLOSTERIC REGULATION; ALPHA7 NICOTINIC ACETYLCHOLINE RECEPTOR; AMINO ACID SEQUENCE; CELL MEMBRANE; EXTRACELLULAR SPACE; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS;

EID: 84901044877     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.524611     Document Type: Article

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