Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate

Research output: Contribution to journalJournal articlepeer-review

Standard

Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate. / Kristensen, Ole; Kristensen, Lise Baadsgaard; Møllerud, Stine; Frydenvang, Karla Andrea; Pickering, Darryl S; Kastrup, Jette Sandholm Jensen.

In: Structure, Vol. 24, No. 9, 2016, p. 1582-1589.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Kristensen, O, Kristensen, LB, Møllerud, S, Frydenvang, KA, Pickering, DS & Kastrup, JSJ 2016, 'Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate', Structure, vol. 24, no. 9, pp. 1582-1589. https://doi.org/10.1016/j.str.2016.06.019

APA

Kristensen, O., Kristensen, L. B., Møllerud, S., Frydenvang, K. A., Pickering, D. S., & Kastrup, J. S. J. (2016). Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate. Structure, 24(9), 1582-1589. https://doi.org/10.1016/j.str.2016.06.019

Vancouver

Kristensen O, Kristensen LB, Møllerud S, Frydenvang KA, Pickering DS, Kastrup JSJ. Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate. Structure. 2016;24(9):1582-1589. https://doi.org/10.1016/j.str.2016.06.019

Author

Kristensen, Ole ; Kristensen, Lise Baadsgaard ; Møllerud, Stine ; Frydenvang, Karla Andrea ; Pickering, Darryl S ; Kastrup, Jette Sandholm Jensen. / Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate. In: Structure. 2016 ; Vol. 24, No. 9. pp. 1582-1589.

Bibtex

@article{2051c9545bf148c1befeae90dd3bf2a1,
title = "Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate",
abstract = "Ionotropic glutamate receptors play a key role for fast neurotransmission in the central nervous system and have been linked to several neurological diseases and disorders. One subfamily is the kainate receptors that are grouped into low-affinity (GluK1-3) and high-affinity (GluK4-5) receptors based on their affinity for kainate. Whereas structures of the ligand-binding domain (LBD) of all low-affinity kainate receptors have been reported, no structures are available of the high-affinity receptor subunits. Here, we present the X-ray structure of GluK4-LBD with kainate at 2.05 {\AA} resolution, together with thermofluor and radiolabel binding affinity data. Whereas binding site residues in GluK4 are most similar to the AMPA receptor subfamily, the domain closure and D1-D2 interlobe contacts induced by kainate is similar to the low-affinity kainate receptor GluK1. These observations provide a likely explanation for the high binding affinity of kainate at GluK4-LBD.",
author = "Ole Kristensen and Kristensen, {Lise Baadsgaard} and Stine M{\o}llerud and Frydenvang, {Karla Andrea} and Pickering, {Darryl S} and Kastrup, {Jette Sandholm Jensen}",
year = "2016",
doi = "10.1016/j.str.2016.06.019",
language = "English",
volume = "24",
pages = "1582--1589",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "9",

}

RIS

TY - JOUR

T1 - Structure of a High-Affinity Kainate Receptor: GluK4 Ligand-Binding Domain Crystallized with Kainate

AU - Kristensen, Ole

AU - Kristensen, Lise Baadsgaard

AU - Møllerud, Stine

AU - Frydenvang, Karla Andrea

AU - Pickering, Darryl S

AU - Kastrup, Jette Sandholm Jensen

PY - 2016

Y1 - 2016

N2 - Ionotropic glutamate receptors play a key role for fast neurotransmission in the central nervous system and have been linked to several neurological diseases and disorders. One subfamily is the kainate receptors that are grouped into low-affinity (GluK1-3) and high-affinity (GluK4-5) receptors based on their affinity for kainate. Whereas structures of the ligand-binding domain (LBD) of all low-affinity kainate receptors have been reported, no structures are available of the high-affinity receptor subunits. Here, we present the X-ray structure of GluK4-LBD with kainate at 2.05 Å resolution, together with thermofluor and radiolabel binding affinity data. Whereas binding site residues in GluK4 are most similar to the AMPA receptor subfamily, the domain closure and D1-D2 interlobe contacts induced by kainate is similar to the low-affinity kainate receptor GluK1. These observations provide a likely explanation for the high binding affinity of kainate at GluK4-LBD.

AB - Ionotropic glutamate receptors play a key role for fast neurotransmission in the central nervous system and have been linked to several neurological diseases and disorders. One subfamily is the kainate receptors that are grouped into low-affinity (GluK1-3) and high-affinity (GluK4-5) receptors based on their affinity for kainate. Whereas structures of the ligand-binding domain (LBD) of all low-affinity kainate receptors have been reported, no structures are available of the high-affinity receptor subunits. Here, we present the X-ray structure of GluK4-LBD with kainate at 2.05 Å resolution, together with thermofluor and radiolabel binding affinity data. Whereas binding site residues in GluK4 are most similar to the AMPA receptor subfamily, the domain closure and D1-D2 interlobe contacts induced by kainate is similar to the low-affinity kainate receptor GluK1. These observations provide a likely explanation for the high binding affinity of kainate at GluK4-LBD.

U2 - 10.1016/j.str.2016.06.019

DO - 10.1016/j.str.2016.06.019

M3 - Journal article

C2 - 27524200

VL - 24

SP - 1582

EP - 1589

JO - Structure

JF - Structure

SN - 0969-2126

IS - 9

ER -

ID: 163109368