NMR structure and dynamics of the agonist dynorphin peptide bound to the human kappa opioid receptor

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

Volumn 112, Issue 38, 2015, Pages 11852-11857

  O'Connor, Casey ^a,b   White, Kate L ^a,b,c   Doncescu, Nathalie ^d   Didenko, Tatiana ^a   Roth, Bryan L ^c   Czaplicki, Georges ^d   Stevens, Raymond C ^a,b   Wüthrich, Kurt ^a,e   Milon, Alain ^a,d   Summers, Michael F ^f  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

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

^d UNIVERSITÉ PAUL SABATIER   (France)

^e ETH ZURICH   (Switzerland)

^f UNIVERSITY OF MARYLAND BALTIMORE COUNTY   (United States)

Author keywords

15N relaxation; GPCR activation; Ligand binding affinity; Molecular dynamics simulations; Transferred NOE

Indexed keywords

DYNORPHIN; G PROTEIN COUPLED RECEPTOR; KAPPA OPIATE RECEPTOR; RADIOLIGAND; 7-HYDROXY-N-(1-((4-(3-HYDROXYPHENYL)-3,4-DIMETHYL-1-PIPERIDINYL)METHYL)-2-METHYLPROPYL)-1,2,3,4-TETRAHYDRO-3-ISOQUINOLINECARBOXAMIDE; DYNORPHIN (1-13); LIGAND; NITROGEN; PEPTIDE; PEPTIDE FRAGMENT; PIPERIDINE DERIVATIVE; PROTEIN BINDING; TETRAHYDROISOQUINOLINE DERIVATIVE;

AMINO TERMINAL SEQUENCE; ANALYTIC METHOD; ARTICLE; BINDING AFFINITY; CARBON NUCLEAR MAGNETIC RESONANCE; CARBOXY TERMINAL SEQUENCE; LIGAND BINDING; MOLECULAR DYNAMICS; MOLECULAR MODEL; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; AGONISTS; AMINO ACID SEQUENCE; CHEMISTRY; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE; TIME FACTOR;

AMINO ACID SEQUENCE; DYNORPHINS; HUMANS; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR DYNAMICS SIMULATION; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; PEPTIDE FRAGMENTS; PEPTIDES; PIPERIDINES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, OPIOID, KAPPA; TETRAHYDROISOQUINOLINES; TIME FACTORS;

EID: 84942896526     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1510117112     Document Type: Article

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