Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Standard

Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators. / Pøhlsgaard, Jacob; Frydenvang, Karla Andrea; Madsen, Ulf; Kastrup, Jette Sandholm.

I: Neuropharmacology, Bind 60, Nr. 1, 01.01.2011, s. 135-150.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Pøhlsgaard, J, Frydenvang, KA, Madsen, U & Kastrup, JS 2011, 'Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators', Neuropharmacology, bind 60, nr. 1, s. 135-150. https://doi.org/10.1016/j.neuropharm.2010.08.004

APA

Pøhlsgaard, J., Frydenvang, K. A., Madsen, U., & Kastrup, J. S. (2011). Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators. Neuropharmacology, 60(1), 135-150. https://doi.org/10.1016/j.neuropharm.2010.08.004

Vancouver

Pøhlsgaard J, Frydenvang KA, Madsen U, Kastrup JS. Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators. Neuropharmacology. 2011 jan. 1;60(1):135-150. https://doi.org/10.1016/j.neuropharm.2010.08.004

Author

Pøhlsgaard, Jacob ; Frydenvang, Karla Andrea ; Madsen, Ulf ; Kastrup, Jette Sandholm. / Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators. I: Neuropharmacology. 2011 ; Bind 60, Nr. 1. s. 135-150.

Bibtex

@article{14afb86d372443389c41e5aca7f97d30,
title = "Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators",
abstract = "Ionotropic glutamate receptors (iGluRs) constitute a family of ligand-gated ion channels that are essential for mediating fast synaptic transmission in the central nervous system. These receptors play an important role for the development and function of the nervous system, and are essential in learning and memory. However, iGluRs are also implicated in or have causal roles for several brain disorders, e.g. epilepsy, Alzheimer's disease, Parkinson's disease and schizophrenia. Their involvement in neurological diseases has stimulated widespread interest in their structure and function. Since the first publication in 1998 of the structure of a recombinant soluble protein comprising the ligand-binding domain of GluA2 extensive studies have afforded numerous crystal structures of wildtype and mutant proteins including different ligands. The structural information obtained combined with functional data have led to models for receptor activation and desensitization by agonists, inhibition by antagonists and block of desensitization by positive allosteric modulators. Furthermore, the structural and functional studies have formed a powerful platform for the design of new selective compounds.",
keywords = "Former Faculty of Pharmaceutical Sciences",
author = "Jacob P{\o}hlsgaard and Frydenvang, {Karla Andrea} and Ulf Madsen and Kastrup, {Jette Sandholm}",
note = "Keywords: GluA2, ligand-binding domain, agonist, antagonist, positive allosteric modulator, crystal structure",
year = "2011",
month = jan,
day = "1",
doi = "10.1016/j.neuropharm.2010.08.004",
language = "English",
volume = "60",
pages = "135--150",
journal = "Neuropharmacology",
issn = "0028-3908",
publisher = "Pergamon Press",
number = "1",

}

RIS

TY - JOUR

T1 - Lessons from more than 80 structures of the GluA2 ligand-binding domain in complex with agonists, antagonists and allosteric modulators

AU - Pøhlsgaard, Jacob

AU - Frydenvang, Karla Andrea

AU - Madsen, Ulf

AU - Kastrup, Jette Sandholm

N1 - Keywords: GluA2, ligand-binding domain, agonist, antagonist, positive allosteric modulator, crystal structure

PY - 2011/1/1

Y1 - 2011/1/1

N2 - Ionotropic glutamate receptors (iGluRs) constitute a family of ligand-gated ion channels that are essential for mediating fast synaptic transmission in the central nervous system. These receptors play an important role for the development and function of the nervous system, and are essential in learning and memory. However, iGluRs are also implicated in or have causal roles for several brain disorders, e.g. epilepsy, Alzheimer's disease, Parkinson's disease and schizophrenia. Their involvement in neurological diseases has stimulated widespread interest in their structure and function. Since the first publication in 1998 of the structure of a recombinant soluble protein comprising the ligand-binding domain of GluA2 extensive studies have afforded numerous crystal structures of wildtype and mutant proteins including different ligands. The structural information obtained combined with functional data have led to models for receptor activation and desensitization by agonists, inhibition by antagonists and block of desensitization by positive allosteric modulators. Furthermore, the structural and functional studies have formed a powerful platform for the design of new selective compounds.

AB - Ionotropic glutamate receptors (iGluRs) constitute a family of ligand-gated ion channels that are essential for mediating fast synaptic transmission in the central nervous system. These receptors play an important role for the development and function of the nervous system, and are essential in learning and memory. However, iGluRs are also implicated in or have causal roles for several brain disorders, e.g. epilepsy, Alzheimer's disease, Parkinson's disease and schizophrenia. Their involvement in neurological diseases has stimulated widespread interest in their structure and function. Since the first publication in 1998 of the structure of a recombinant soluble protein comprising the ligand-binding domain of GluA2 extensive studies have afforded numerous crystal structures of wildtype and mutant proteins including different ligands. The structural information obtained combined with functional data have led to models for receptor activation and desensitization by agonists, inhibition by antagonists and block of desensitization by positive allosteric modulators. Furthermore, the structural and functional studies have formed a powerful platform for the design of new selective compounds.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1016/j.neuropharm.2010.08.004

DO - 10.1016/j.neuropharm.2010.08.004

M3 - Review

C2 - 20713069

VL - 60

SP - 135

EP - 150

JO - Neuropharmacology

JF - Neuropharmacology

SN - 0028-3908

IS - 1

ER -

ID: 33024009