Conformational dynamics of a G-protein α subunit is tightly regulated by nucleotide binding

Proceedings of the National Academy of Sciences of the United States of America

Volumn 113, Issue 26, 2016, Pages E3629-E3638

  Goricanec, David ^a,b   Stehle, Ralf ^a,b   Egloff, Pascal ^c   Grigoriu, Simina ^d   Plückthun, Andreas ^c   Wagner, Gerhard ^a,d   Hagn, Franz ^a,b,d  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b INSTITUTE OF EPIDEMIOLOGY   (Germany)

^c UNIVERSITY OF ZURICH   (Switzerland)

^d HARVARD MEDICAL SCHOOL   (United States)

Author keywords

GPCR; NMR; SAXS; Signaling; Structure

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MEMBRANE SCAFFOLD PROTEIN 1D1; NEUROTENSIN RECEPTOR; RAS PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; G PROTEIN COUPLED RECEPTOR; GNAI1 PROTEIN, HUMAN; HETEROTRIMERIC GUANINE NUCLEOTIDE BINDING PROTEIN; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN BINDING;

ARTICLE; ASSOCIATION RATE CONSTANT; BETA SHEET; CARBON NUCLEAR MAGNETIC RESONANCE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HYDROGEN BOND; HYDROPHOBICITY; LOW TEMPERATURE; MELTING POINT; MOLECULAR DYNAMICS; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE BINDING SITE; PHOSPHOLIPID BILAYER; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; RADIATION SCATTERING; TRANSVERSE RELAXATION OPTIMIZED SPECTROSCOPY; X RAY CRYSTALLOGRAPHY; CHEMISTRY; HUMAN; METABOLISM; SIGNAL TRANSDUCTION;

CRYSTALLOGRAPHY, X-RAY; GTP-BINDING PROTEIN ALPHA SUBUNITS, GI-GO; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HETEROTRIMERIC GTP-BINDING PROTEINS; HUMANS; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTORS, G-PROTEIN-COUPLED; SIGNAL TRANSDUCTION;

EID: 84976498319     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1604125113     Document Type: Article

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