Lessons from crystal structures of kainate receptors

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Lessons from crystal structures of kainate receptors. / Møllerud, Stine; Frydenvang, Karla Andrea; Pickering, Darryl S; Kastrup, Jette Sandholm Jensen.

In: Neuropharmacology, Vol. 112, No. Part A, 01.01.2017, p. 16-28.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Møllerud, S, Frydenvang, KA, Pickering, DS & Kastrup, JSJ 2017, 'Lessons from crystal structures of kainate receptors', Neuropharmacology, vol. 112, no. Part A, pp. 16-28. https://doi.org/10.1016/j.neuropharm.2016.05.014

APA

Møllerud, S., Frydenvang, K. A., Pickering, D. S., & Kastrup, J. S. J. (2017). Lessons from crystal structures of kainate receptors. Neuropharmacology, 112(Part A), 16-28. https://doi.org/10.1016/j.neuropharm.2016.05.014

Vancouver

Møllerud S, Frydenvang KA, Pickering DS, Kastrup JSJ. Lessons from crystal structures of kainate receptors. Neuropharmacology. 2017 Jan 1;112(Part A):16-28. https://doi.org/10.1016/j.neuropharm.2016.05.014

Author

Møllerud, Stine ; Frydenvang, Karla Andrea ; Pickering, Darryl S ; Kastrup, Jette Sandholm Jensen. / Lessons from crystal structures of kainate receptors. In: Neuropharmacology. 2017 ; Vol. 112, No. Part A. pp. 16-28.

Bibtex

@article{6d1178e98704414583612ef0784d4397,
title = "Lessons from crystal structures of kainate receptors",
abstract = "Kainate receptors belong to the family of ionotropic glutamate receptors. These receptors assemble from five subunits (GluK1-5) into tetrameric ion channels. Kainate receptors are located at both pre- and postsynaptic membranes in the central nervous system where they contribute to excitatory synaptic transmission and modulate network excitability by regulating neurotransmitter release. Dysfunction of kainate receptors has been implicated in several neurological disorders such as epilepsy, schizophrenia and depression. Here we provide a review on the current understanding of kainate receptor structure and how they bind agonists, antagonists and ions. The first structure of the ligand-binding domain of the GluK1 subunit was reported in 2005, seven years after publication of the crystal structure of a soluble construct of the ligand-binding domain of the AMPA-type subunit GluA2. Today, a full-length structure has been determined of GluK2 by cryo electron microscopy to 7.6 {\AA} resolution as well as 84 high-resolution crystal structures of N-terminal domains and ligand-binding domains, including agonist and antagonist bound structures, modulatory ions and mutations. However, there are still many unanswered questions and challenges in front of us.",
author = "Stine M{\o}llerud and Frydenvang, {Karla Andrea} and Pickering, {Darryl S} and Kastrup, {Jette Sandholm Jensen}",
year = "2017",
month = "1",
day = "1",
doi = "10.1016/j.neuropharm.2016.05.014",
language = "English",
volume = "112",
pages = "16--28",
journal = "Neuropharmacology",
issn = "0028-3908",
publisher = "Pergamon Press",
number = "Part A",

}

RIS

TY - JOUR

T1 - Lessons from crystal structures of kainate receptors

AU - Møllerud, Stine

AU - Frydenvang, Karla Andrea

AU - Pickering, Darryl S

AU - Kastrup, Jette Sandholm Jensen

PY - 2017/1/1

Y1 - 2017/1/1

N2 - Kainate receptors belong to the family of ionotropic glutamate receptors. These receptors assemble from five subunits (GluK1-5) into tetrameric ion channels. Kainate receptors are located at both pre- and postsynaptic membranes in the central nervous system where they contribute to excitatory synaptic transmission and modulate network excitability by regulating neurotransmitter release. Dysfunction of kainate receptors has been implicated in several neurological disorders such as epilepsy, schizophrenia and depression. Here we provide a review on the current understanding of kainate receptor structure and how they bind agonists, antagonists and ions. The first structure of the ligand-binding domain of the GluK1 subunit was reported in 2005, seven years after publication of the crystal structure of a soluble construct of the ligand-binding domain of the AMPA-type subunit GluA2. Today, a full-length structure has been determined of GluK2 by cryo electron microscopy to 7.6 Å resolution as well as 84 high-resolution crystal structures of N-terminal domains and ligand-binding domains, including agonist and antagonist bound structures, modulatory ions and mutations. However, there are still many unanswered questions and challenges in front of us.

AB - Kainate receptors belong to the family of ionotropic glutamate receptors. These receptors assemble from five subunits (GluK1-5) into tetrameric ion channels. Kainate receptors are located at both pre- and postsynaptic membranes in the central nervous system where they contribute to excitatory synaptic transmission and modulate network excitability by regulating neurotransmitter release. Dysfunction of kainate receptors has been implicated in several neurological disorders such as epilepsy, schizophrenia and depression. Here we provide a review on the current understanding of kainate receptor structure and how they bind agonists, antagonists and ions. The first structure of the ligand-binding domain of the GluK1 subunit was reported in 2005, seven years after publication of the crystal structure of a soluble construct of the ligand-binding domain of the AMPA-type subunit GluA2. Today, a full-length structure has been determined of GluK2 by cryo electron microscopy to 7.6 Å resolution as well as 84 high-resolution crystal structures of N-terminal domains and ligand-binding domains, including agonist and antagonist bound structures, modulatory ions and mutations. However, there are still many unanswered questions and challenges in front of us.

U2 - 10.1016/j.neuropharm.2016.05.014

DO - 10.1016/j.neuropharm.2016.05.014

M3 - Journal article

C2 - 27236079

VL - 112

SP - 16

EP - 28

JO - Neuropharmacology

JF - Neuropharmacology

SN - 0028-3908

IS - Part A

ER -

ID: 163106098