期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 22, 期 3, 页码 265-268出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2965
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资金
- US National Institutes of Health (NIH)
- National Institute of General Medical Sciences grant [U54 GM094618, R01 GM108635, U54 GM094599, R01 GM095583, P41 GM103393]
- US National Institute of Drug Abuse grant [P01 DA035764, R01 DA017204]
- US National Institute of Mental Health Psychoactive Drug Screening Program
- Michael Hooker Chair for Protein Therapeutics and Translational Proteomics
- US National Science Foundation Science and Technology Center award [1231306]
- Helmholtz Association
- German Research Foundation (DFG) Cluster of Excellence 'Center for Ultrafast Imaging'
- German Federal Ministry of Education and Research (BMBF) project [FKZ 05K12CH1, 05K2012]
- PIER Helmholtz Graduate School
- Marie Curie Initial Training Network NanoMem [317079]
- Ministere du Developpement Economique, de l'Innovation et de l'Exportation du Quebec [PSR-SIIRI-417]
- Research Foundation-Flanders (FWO Vlaanderen) [FWOAL570]
- Canadian Institutes of Health Research (CIHR) [MOP-89716]
- NIH [DA-004443]
- US National Cancer Institute grant [Y1-CO-1020]
- US National Institute of General Medical Sciences grant [Y1-GM-1104]
Bifunctional mu- and delta-opioid receptor (OR) ligands are potential therapeutic alternatives, with diminished side effects, to alkaloid opiate analgesics. We solved the structure of human delta-OR bound to the bifunctional delta-OR antagonist and mu-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.
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