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Article

The interaction of highly helical structural mutants with the NOP receptor discloses the role of the address domain of nociceptin/orphanin FQ.

Chemistry (Weinheim an der Bergstrasse, Germany) - 18 Mar 2005

Tancredi Teodorico, Carrà Giacomo, Guerrini Remo, Arduin Marika, Calò Girolamo, Regoli Domenico, Salvadori Severo, Temussi Piero Andrea

Abstract excerpt

Nociceptin is a heptadecapeptide whose sequence is similar to that of Dynorphin A, sharing a message domain characterized by two glycines and two aromatic residues, and a highly basic C-terminal address domain but, in spite of these similarities, displays no opioid activity. Establishing the relative importance of the message and address domains of nociceptin has so far been hampered by its extreme conformational...

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Identifiers

PMID: 15712334
DOI: 10.1002/chem.200401095

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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