6jmv

From Proteopedia

Crystal structure of the GluK3 ligand binding domain complex with SYM and zinc

PDB ID 6jmv

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Structural highlights

6jmv is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.832Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GRIK3_RAT Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA.^[1]

Publication Abstract from PubMed

GluK3-kainate receptors are atypical members of the iGluR family that reside at both the pre- and postsynapse and play a vital role in the regulation of synaptic transmission. For a better understanding of structural changes that underlie receptor functions, GluK3 receptors were trapped in desensitized and resting/closed states and structures analyzed using single particle cryo-electron microscopy. While the desensitized GluK3 has domain organization as seen earlier for another kainate receptor-GluK2, antagonist bound GluK3 trapped a resting state with only two LBD domains in dimeric arrangement necessary for receptor activation. Using structures as a guide, we show that the N-linked glycans at the interface of GluK3 ATD and LBD likely mediate inter-domain interactions and attune receptor-gating properties. The mutational analysis also identified putative N-glycan interacting residues. Our results provide a molecular framework for understanding gating properties unique to GluK3 and exploring the role of N-linked glycosylation in their modulation.

Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery.,Kumari J, Vinnakota R, Kumar J Sci Rep. 2019 Jul 16;9(1):10254. doi: 10.1038/s41598-019-46770-z. PMID:31311973^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Venskutonyte R, Frydenvang K, Gajhede M, Bunch L, Pickering DS, Kastrup JS. Binding site and interlobe interactions of the ionotropic glutamate receptor GluK3 ligand binding domain revealed by high resolution crystal structure in complex with (S)-glutamate. J Struct Biol. 2011 Sep 1. PMID:21907808 doi:10.1016/j.jsb.2011.08.014
↑ Kumari J, Vinnakota R, Kumar J. Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery. Sci Rep. 2019 Jul 16;9(1):10254. doi: 10.1038/s41598-019-46770-z. PMID:31311973 doi:http://dx.doi.org/10.1038/s41598-019-46770-z