5ehs: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of the Drosophila CG3822 KaiR1D ligand binding domain complex with D-AP5== | ==Crystal structure of the Drosophila CG3822 KaiR1D ligand binding domain complex with D-AP5== | ||
<StructureSection load='5ehs' size='340' side='right' caption='[[5ehs]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='5ehs' size='340' side='right'caption='[[5ehs]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ehs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EHS OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5ehs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drogr Drogr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EHS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EHS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2JJ:5-PHOSPHONO-D-NORVALINE'>2JJ</scene>, <scene name='pdbligand=5OY:5-PHOSPHONO-L-NORVALINE'>5OY</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2JJ:5-PHOSPHONO-D-NORVALINE'>2JJ</scene>, <scene name='pdbligand=5OY:5-PHOSPHONO-L-NORVALINE'>5OY</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dtb|5dtb]], [[5ehm|5ehm]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dtb|5dtb]], [[5ehm|5ehm]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dgri\GH17276, Dgri_GH17276, GH17276 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7222 DROGR])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ehs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ehs OCA], [http://pdbe.org/5ehs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ehs RCSB], [http://www.ebi.ac.uk/pdbsum/5ehs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ehs ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 21: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Drogr]] | |||
[[Category: Large Structures]] | |||
[[Category: Dharkar, P]] | [[Category: Dharkar, P]] | ||
[[Category: Mayer, M L]] | [[Category: Mayer, M L]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
Revision as of 09:58, 22 April 2020
Crystal structure of the Drosophila CG3822 KaiR1D ligand binding domain complex with D-AP5Crystal structure of the Drosophila CG3822 KaiR1D ligand binding domain complex with D-AP5
Structural highlights
Publication 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
|
| ||||||||||||||||||||