Skip to main content
Advertisement

Main menu

  • Home
  • Articles
    • Current Issue
    • Fast Forward
    • Latest Articles
    • 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
  • 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
    • 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
  • Visit molpharm on Facebook
  • Follow molpharm on Twitter
  • Follow molpharm on LinkedIn

Cover Caption

About the cover: Putative structure of a regulatory domain in the amino terminus of the N-methyl-D-aspartate (NMDA) receptor NR1 subunit. The left-hand schematic shows the proposed topology of the NMDA receptor subunits with three membrane-spanning domains, a re-entrant loop, the agonist binding pocket formed by the S1-S2 domains (with the agonist shown by a gray oval), and a large extracellular amino terminus that precedes S1. The positions of amino acid residues that may form binding sites for ifenprodil (green) and spermine (yellow) are shown by circles. The right-hand schematic is a projected structure of the bacterial leucine/isoleucine/valine binding protein (LIVBP). The putative secondary structure of the amino terminus of NR1 shows considerable similarity to that of LIVBP, and this region of NR1, which is termed the R1-R2 regulatory domain, is proposed to have a tertiary structure similar to LIVBP. From Masuko T, Kashiwagi K, Kuno T, Nguyen ND, Pahk AJ, Fukuchi J-I, Igarashi K and Williams K (1999) A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D-aspartate receptor: Effects of spermine, protons, and ifenprodil, and structural similarity to bacterial LIVBP. Mol Pharmacol 55:957-969.

Back to top
PreviousNext

In this issue

Molecular Pharmacology: 56 (6)
Molecular Pharmacology
Vol. 56, Issue 6
1 Dec 1999
  • Table of Contents
  • About the Cover
  • Index by author
Sign up for alerts

Jump to

  • Articles
  • Accelerated Communication
  • Erratum
  • Most Read
Loading
  • How Many G Protein-Coupled Receptors are Drug Targets?
  • Nelfinavir and PXR
  • Wnt Signaling and Drug Resistance in Cancer
  • Coronavirus in the Brain and the Impact of Smoking
  • Arginine-259 of UGT2B7 Confers UDP-Sugar Selectivity
More...
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 © 2021 by the American Society for Pharmacology and Experimental Therapeutics