Solution Conformation of Nociceptin |
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| Affiliation: | 1. Laboratory of Plant Cytophysiology, Department of Environmental and Prevention Sciences, University of Ferrara, Ferrara, Italy;2. Department of Plant Physiology, Slovak University of Agriculture, Nitra, Slovakia;3. K.A. Timiryazev Institute of Plant Physiology, RAS, Botanicheskaya Street 35, Moscow 127276, Russia |
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| Abstract: | Nociceptin, a novel heptadecapeptide, interacts with ORL1a G protein-coupled receptor whose sequence is closely related to that of the κ opioid receptor but has no opioid activity. We have investigated the conformational preferences of Nociceptin also in comparison to Dynorphin A. The N-terminal part of Nociceptin has the same conformational preferences of the message of endogenous opioids but the C-terminal part of the sequence is more flexible than the corresponding address of Dynorphin A. [Tyr1]-Nociceptin, while retaining nociceptive activity, has also an opioid activity comparable to that of enkephalins. |
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