Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation

Nature

Volumn 535, Issue 7612, 2016, Pages 448-452

  Staus, Dean P ^a   Strachan, Ryan T ^b   Manglik, Aashish ^c   Pani, Biswaranjan ^a   Kahsai, Alem W ^a   Kim, Tae Hun ^d   Wingler, Laura M ^a   Ahn, Seungkirl ^a   Chatterjee, Arnab ^a   Masoudi, Ali ^a   Kruse, Andrew C ^e   Pardon, Els ^f,g   Steyaert, Jan ^f,g   Weis, William I ^c   Prosser, R Scott ^d   Kobilka, Brian K ^c   Costa, Tommaso ^h   Lefkowitz, Robert J ^a,i  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d UNIVERSITY OF TORONTO   (Canada)

^e HARVARD MEDICAL SCHOOL   (United States)

^f VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^g DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^h ISTITUTO SUPERIORE DI SANITÀ   (Italy)

ⁱ HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; G PROTEIN COUPLED RECEPTOR; NANOBODY; PARTIAL AGONIST; BETA 2 ADRENERGIC RECEPTOR STIMULATING AGENT; ISOPRENALINE; LIGAND;

CELLS AND CELL COMPONENTS; CRYSTALLOGRAPHY; EXPERIMENTAL STUDY; NANOPARTICLE; PROTEIN; STABILIZATION;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; DISPERSION; EQUILIBRIUM CONSTANT; INTRACELLULAR SIGNALING; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INDUCTION; BINDING SITE; CHEMISTRY; DRUG EFFECTS; HUMAN; METABOLISM; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; PARTIAL AGONISM; PROTEIN STABILITY; X RAY CRYSTALLOGRAPHY;

CAMELIDAE;

ADRENERGIC BETA-2 RECEPTOR AGONISTS; ALLOSTERIC REGULATION; ALLOSTERIC SITE; CRYSTALLOGRAPHY, X-RAY; DRUG PARTIAL AGONISM; HUMANS; ISOPROTERENOL; LIGANDS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN STABILITY; RECEPTORS, ADRENERGIC, BETA-2; SINGLE-DOMAIN ANTIBODIES;

EID: 84978080610     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature18636     Document Type: Article

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