5dtb: Difference between revisions
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==Crystal structure of the Drosophila CG3822 KaiR1D ligand binding domain complex with glutamate== | |||
<StructureSection load='5dtb' size='340' side='right'caption='[[5dtb]], [[Resolution|resolution]] 1.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dtb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DTB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.843Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dtb OCA], [https://pdbe.org/5dtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dtb RCSB], [https://www.ebi.ac.uk/pdbsum/5dtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dtb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9VDH5_DROME Q9VDH5_DROME] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phylogenetic analysis reveals AMPA, kainate, and NMDA receptor families in insect genomes, suggesting conserved functional properties corresponding to their vertebrate counterparts. However, heterologous expression of the Drosophila kainate receptor DKaiR1D and the AMPA receptor DGluR1A revealed novel ligand selectivity at odds with the classification used for vertebrate glutamate receptor ion channels (iGluRs). DKaiR1D forms a rapidly activating and desensitizing receptor that is inhibited by both NMDA and the NMDA receptor antagonist AP5; crystallization of the KaiR1D ligand-binding domain reveals that these ligands stabilize open cleft conformations, explaining their action as antagonists. Surprisingly, the AMPA receptor DGluR1A shows weak activation by its namesake agonist AMPA and also by quisqualate. Crystallization of the DGluR1A ligand-binding domain reveals amino acid exchanges that interfere with binding of these ligands. The unexpected ligand-binding profiles of insect iGluRs allows classical tools to be used in novel approaches for the study of synaptic regulation. VIDEO ABSTRACT. | |||
Novel Functional Properties of Drosophila CNS Glutamate Receptors.,Li Y, Dharkar P, Han TH, Serpe M, Lee CH, Mayer ML Neuron. 2016 Dec 7;92(5):1036-1048. doi: 10.1016/j.neuron.2016.10.058. Epub 2016 , Nov 23. PMID:27889096<ref>PMID:27889096</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5dtb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Drosophila melanogaster]] | |||
[[Category: Large Structures]] | |||
[[Category: Dharkar P]] | |||
[[Category: Mayer ML]] | |||
Latest revision as of 00:58, 29 June 2023
Crystal structure of the Drosophila CG3822 KaiR1D ligand binding domain complex with glutamateCrystal structure of the Drosophila CG3822 KaiR1D ligand binding domain complex with glutamate
Structural highlights
FunctionPublication Abstract from PubMedPhylogenetic analysis reveals AMPA, kainate, and NMDA receptor families in insect genomes, suggesting conserved functional properties corresponding to their vertebrate counterparts. However, heterologous expression of the Drosophila kainate receptor DKaiR1D and the AMPA receptor DGluR1A revealed novel ligand selectivity at odds with the classification used for vertebrate glutamate receptor ion channels (iGluRs). DKaiR1D forms a rapidly activating and desensitizing receptor that is inhibited by both NMDA and the NMDA receptor antagonist AP5; crystallization of the KaiR1D ligand-binding domain reveals that these ligands stabilize open cleft conformations, explaining their action as antagonists. Surprisingly, the AMPA receptor DGluR1A shows weak activation by its namesake agonist AMPA and also by quisqualate. Crystallization of the DGluR1A ligand-binding domain reveals amino acid exchanges that interfere with binding of these ligands. The unexpected ligand-binding profiles of insect iGluRs allows classical tools to be used in novel approaches for the study of synaptic regulation. VIDEO ABSTRACT. Novel Functional Properties of Drosophila CNS Glutamate Receptors.,Li Y, Dharkar P, Han TH, Serpe M, Lee CH, Mayer ML Neuron. 2016 Dec 7;92(5):1036-1048. doi: 10.1016/j.neuron.2016.10.058. Epub 2016 , Nov 23. PMID:27889096[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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