Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:3.28
Classification:MEMBRANE PROTEIN
Release Date:2015-01-14
Deposition Date:2014-12-01
Revision Date:2015-04-01#2017-06-07#2017-11-22
Molecular Weight:92951.73
Macromolecule Type:Protein
Residue Count:832
Atom Site Count:5933
DOI:10.2210/pdb4rwa/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.
Resolution:3.28
Classification:MEMBRANE PROTEIN
Release Date:2015-01-14
Deposition Date:2014-12-01
Revision Date:2015-04-01#2017-06-07#2017-11-22
Molecular Weight:92951.73
Macromolecule Type:Protein
Residue Count:832
Atom Site Count:5933
DOI:10.2210/pdb4rwa/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 available | 2015 |
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Publisher | RCSB-PDB |