4RWD : XFEL structure of the human delta opioid receptor in complex with a bifunctional peptide

  • Raymond C. Stevens (Contributor)
  • Raymond C. Stevens (Contributor)
  • Chelsie E. Conrad (Contributor)
  • Petra Fromme (Contributor)
  • Bryan L. Roth (Contributor)
  • Jesse Coe (Contributor)
  • Peter W. Schiller (Contributor)
  • Vsevolod Katritch (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.7
Classification:MEMBRANE PROTEIN
Release Date:2015-01-14
Deposition Date:2014-12-02
Revision Date:2015-04-01#2017-06-07#2018-02-14
Molecular Weight:95688.02
Macromolecule Type:Protein
Residue Count:832
Atom Site Count:6299
DOI:10.2210/pdb4rwd/pdb

Abstract:
Bifunctional μ- and δ-opioid receptor (OR) ligands are potential therapeutic alternatives, with diminished side effects, to alkaloid opiate analgesics. We solved the structure of human δ-OR bound to the bifunctional δ-OR antagonist and μ-OR agonist tetrapeptide H-Dmt-Tic-Phe-Phe-NH2 (DIPP-NH2) by serial femtosecond crystallography, revealing a cis-peptide bond between H-Dmt and Tic. The observed receptor-peptide interactions are critical for understanding of the pharmacological profiles of opioid peptides and for development of improved analgesics.
Date made availableJan 14 2015
PublisherRCSB-PDB

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