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Structural basis for bifunctional peptide recognition at human delta-opioid receptor

Academic Article
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Overview

authors

  • Fenalti, G.
  • Zatsepin, N. A.
  • Betti, C.
  • Giguere, P.
  • Han, G. W.
  • Ishchenko, A.
  • Liu, W.
  • Guillemyn, K.
  • Zhang, H.
  • James, D.
  • Wang, D.
  • Weierstall, U.
  • Spence, J. C. H.
  • Boutet, S.
  • Messerschmidt, M.
  • Williams, G. J.
  • Gati, C.
  • Yefanov, O. M.
  • White, T. A.
  • Oberthuer, D.
  • Metz, M.
  • Yoon, C. H.
  • Barty, A.
  • Chapman, H. N.
  • Basu, S.
  • Coe, J.
  • Conrad, C. E.
  • Fromme, R.
  • Fromme, P.
  • Tourwe, D.
  • Schiller, P. W.
  • Roth, B. L.
  • Ballet, S.
  • Katritch, Vsevolod
  • Stevens, Raymond
  • Cherezov, Vadim

publication date

  • March 2015

journal

  • Nature Structural & Molecular Biology  Journal

abstract

  • Bifunctional ?- and ?-opioid receptor (OR) ligands are potential therapeutic alternatives, with diminished side effects, to alkaloid opiate analgesics. We solved the structure of human ?-OR bound to the bifunctional ?-OR antagonist and ?-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.
  • 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.

subject areas

  • Binding Sites
  • Crystallography, X-Ray
  • HEK293 Cells
  • Humans
  • Models, Molecular
  • Oligopeptides
  • Protein Structure, Tertiary
  • Receptors, Opioid, delta
  • Tetrahydroisoquinolines
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Identity

PubMed Central ID

  • PMC4351130

International Standard Serial Number (ISSN)

  • 1545-9993

Digital Object Identifier (DOI)

  • 10.1038/nsmb.2965

PubMed ID

  • 25686086
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Additional Document Info

start page

  • 265

end page

  • 268

volume

  • 22

issue

  • 3

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