Solution structure of dynorphin A (1-17): a NMR study in a cryoprotective solvent mixture at 278 K.
Dynorphin A, the endogenous agonist for the kappa opioid receptor, has been studied by NMR spectroscopy in methanol, acetonitrile, DMSO and in mixtures of hexafluoroacetone/water and DMSO/water. NMR data in the DMSO/water cryomixture at 278 K are consistent with a conformer in which the N-terminal part, like the corresponding message domain of enkephalins, is poorly ordered, whereas the C-terminal part is folded in a loop centred around Pro10. The folded structure of the C-terminal part (address moiety) may shed light on the role of the essential residues Arg7, Lys11 and Lys13.
Spadaccini
R
R
Istituto Chimica MIB del CNR, Napoli, Italy.
Crescenzi
O
O
Picone
D
D
Tancredi
T
T
Temussi
P A
PA
D000595:Amino Acid Sequence; D003080:Cold Temperature; D004399:Dynorphins / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011957:Receptors, Opioid / Q000737:chemistry; D017473:Receptors, Opioid, kappa / Q000737:chemistry; D017450:Receptors, Opioid, mu / Q000737:chemistry; D012996:Solutions; D012997:Solvents; D000094942:Nociceptin Receptor
D011957:Receptors, Opioid; D017473:Receptors, Opioid, kappa; D017450:Receptors, Opioid, mu; D012996:Solutions; D012997:Solvents; D004399:Dynorphins; D000094942:Nociceptin Receptor; C000722283:OPRL1 protein, human