Skip to main content
Advertisement

Main menu

  • Home
  • Articles
    • Current Issue
    • Fast Forward
    • Latest Articles
    • Special Sections
    • Archive
  • Information
    • Instructions to Authors
    • Submit a Manuscript
    • FAQs
    • For Subscribers
    • Terms & Conditions of Use
    • Permissions
  • Editorial Board
  • Alerts
    • Alerts
    • RSS Feeds
  • Virtual Issues
  • Feedback
  • Submit
  • Other Publications
    • Drug Metabolism and Disposition
    • Journal of Pharmacology and Experimental Therapeutics
    • Molecular Pharmacology
    • Pharmacological Reviews
    • Pharmacology Research & Perspectives
    • ASPET

User menu

  • My alerts
  • Log in
  • My Cart

Search

  • Advanced search
Molecular Pharmacology
  • Other Publications
    • Drug Metabolism and Disposition
    • Journal of Pharmacology and Experimental Therapeutics
    • Molecular Pharmacology
    • Pharmacological Reviews
    • Pharmacology Research & Perspectives
    • ASPET
  • My alerts
  • Log in
  • My Cart
Molecular Pharmacology

Advanced Search

  • Home
  • Articles
    • Current Issue
    • Fast Forward
    • Latest Articles
    • Special Sections
    • Archive
  • Information
    • Instructions to Authors
    • Submit a Manuscript
    • FAQs
    • For Subscribers
    • Terms & Conditions of Use
    • Permissions
  • Editorial Board
  • Alerts
    • Alerts
    • RSS Feeds
  • Virtual Issues
  • Feedback
  • Submit
  • Visit molpharm on Facebook
  • Follow molpharm on Twitter
  • Follow molpharm on LinkedIn
Abstract

A single residue, Lys108, of the delta-opioid receptor prevents the mu-opioid-selective ligand [D-Ala2,N-MePhe4,Gly-ol5]enkephalin from binding to the delta-opioid receptor.

M Minami, T Nakagawa, T Seki, T Onogi, Y Aoki, Y Katao, S Katsumata and M Satoh
Molecular Pharmacology November 1996, 50 (5) 1413-1422;
M Minami
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
T Nakagawa
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
T Seki
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
T Onogi
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Y Aoki
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Y Katao
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
S Katsumata
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
M Satoh
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • Article
  • Info & Metrics
  • eLetters
  • PDF
Loading

Abstract

Previously, we found that replacement of the region around the first extracellular loop of the delta-opioid receptor (OPR) with the corresponding region of the mu-OPR gives the high affinity for [D-Ala2,N-MePhe4,Gly-ol5]enkephalin (DAMGO), a mu-opioid-selective ligand, to the resultant chimeric receptor, DMDD, suggesting that the difference in the amino acid sequence within this region between the mu- and delta-OPRs is critical for the discrimination between these receptors by DAMGO. In the current study, we carried out systematic replacements of seven non-conserved residues in this region of the delta-OPR with the corresponding amino acid found in the mu-OPR. Among the seven mutant receptors, only one mutant receptor, delta K108N, showed high affinity (Ki = 18.68 +/- 5.27 nM) for DAMGO, which was comparable to that of the DMDD receptor (Ki = 23.77 +/- 4.27 nM) and 75-fold higher than that of the wild-type delta-OPR (Ki = 1405 +/- 161 nM). Lys108 in the delta-OPR was systematically replaced with 19 kinds of amino acids other than lysine. Among the resultant mutant receptors, 14 mutants bound DAMGO with Ki values comparable to those of the DMDD receptor, ranging from 4.20 to 43.38 nM. These findings suggest that Lys108 of the delta-OPR prevents DAMGO from binding to the delta-OPR rather than that the asparagine residue at the corresponding position in the mu-OPR is necessary for DAMGO binding. In addition, the replacement of Lys108 of the delta-OPR with asparagine dramatically increased the affinity for other peptidic mu receptor-selective ligands, such as dermorphin and D-Pen-Cys-Tyr-D-Trp-Orn-Thr-Pen-Thr-NH2.

MolPharm articles become freely available 12 months after publication, and remain freely available for 5 years. 

Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page. 

 

  • Click here for information on institutional subscriptions.
  • Click here for information on individual ASPET membership.

 

Log in using your username and password

Forgot your user name or password?

Purchase access

You may purchase access to this article. This will require you to create an account if you don't already have one.
PreviousNext
Back to top

In this issue

Molecular Pharmacology
Vol. 50, Issue 5
1 Nov 1996
  • Table of Contents
  • Table of Contents (PDF)
  • Index by author
  • Back Matter (PDF)
  • Editorial Board (PDF)
  • Front Matter (PDF)
Download PDF
Article Alerts
Sign In to Email Alerts with your Email Address
Email Article

Thank you for sharing this Molecular Pharmacology article.

NOTE: We request your email address only to inform the recipient that it was you who recommended this article, and that it is not junk mail. We do not retain these email addresses.

Enter multiple addresses on separate lines or separate them with commas.
A single residue, Lys108, of the delta-opioid receptor prevents the mu-opioid-selective ligand [D-Ala2,N-MePhe4,Gly-ol5]enkephalin from binding to the delta-opioid receptor.
(Your Name) has forwarded a page to you from Molecular Pharmacology
(Your Name) thought you would be interested in this article in Molecular Pharmacology.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Citation Tools
Abstract

A single residue, Lys108, of the delta-opioid receptor prevents the mu-opioid-selective ligand [D-Ala2,N-MePhe4,Gly-ol5]enkephalin from binding to the delta-opioid receptor.

M Minami, T Nakagawa, T Seki, T Onogi, Y Aoki, Y Katao, S Katsumata and M Satoh
Molecular Pharmacology November 1, 1996, 50 (5) 1413-1422;

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero

Share
Abstract

A single residue, Lys108, of the delta-opioid receptor prevents the mu-opioid-selective ligand [D-Ala2,N-MePhe4,Gly-ol5]enkephalin from binding to the delta-opioid receptor.

M Minami, T Nakagawa, T Seki, T Onogi, Y Aoki, Y Katao, S Katsumata and M Satoh
Molecular Pharmacology November 1, 1996, 50 (5) 1413-1422;
del.icio.us logo Digg logo Reddit logo Twitter logo Facebook logo Google logo Mendeley logo
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Jump to section

  • Article
  • Info & Metrics
  • eLetters
  • PDF

Related Articles

Cited By...

Similar Articles

Advertisement
  • Home
  • Alerts
Facebook   Twitter   LinkedIn   RSS

Navigate

  • Current Issue
  • Fast Forward by date
  • Fast Forward by section
  • Latest Articles
  • Archive
  • Search for Articles
  • Feedback
  • ASPET

More Information

  • About Molecular Pharmacology
  • Editorial Board
  • Instructions to Authors
  • Submit a Manuscript
  • Customized Alerts
  • RSS Feeds
  • Subscriptions
  • Permissions
  • Terms & Conditions of Use

ASPET's Other Journals

  • Drug Metabolism and Disposition
  • Journal of Pharmacology and Experimental Therapeutics
  • Pharmacological Reviews
  • Pharmacology Research & Perspectives
ISSN 1521-0111 (Online)

Copyright © 2022 by the American Society for Pharmacology and Experimental Therapeutics