5cfb: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure of Human Glycine Receptor alpha-3 Bound to Strychnine== | ==Crystal Structure of Human Glycine Receptor alpha-3 Bound to Strychnine== | ||
<StructureSection load='5cfb' size='340' side='right' caption='[[5cfb]], [[Resolution|resolution]] 3.04Å' scene=''> | <StructureSection load='5cfb' size='340' side='right'caption='[[5cfb]], [[Resolution|resolution]] 3.04Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cfb]] is a 5 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5cfb]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CFB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SY9:STRYCHNINE'>SY9</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SY9:STRYCHNINE'>SY9</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=5cfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cfb OCA], [https://pdbe.org/5cfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cfb RCSB], [https://www.ebi.ac.uk/pdbsum/5cfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cfb ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GLRA3_HUMAN GLRA3_HUMAN] The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Chen H]] | ||
[[Category: | [[Category: Huang X]] | ||
[[Category: | [[Category: Shaffer PL]] | ||
Revision as of 15:02, 14 June 2023
Crystal Structure of Human Glycine Receptor alpha-3 Bound to StrychnineCrystal Structure of Human Glycine Receptor alpha-3 Bound to Strychnine
Structural highlights
FunctionGLRA3_HUMAN The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing). Publication Abstract from PubMedNeurotransmitter-gated ion channels of the Cys-loop receptor family are essential mediators of fast neurotransmission throughout the nervous system and are implicated in many neurological disorders. Available X-ray structures of prokaryotic and eukaryotic Cys-loop receptors provide tremendous insights into the binding of agonists, the subsequent opening of the ion channel, and the mechanism of channel activation. Yet the mechanism of inactivation by antagonists remains unknown. Here we present a 3.0 A X-ray structure of the human glycine receptor-alpha3 homopentamer in complex with a high affinity, high-specificity antagonist, strychnine. Our structure allows us to explore in detail the molecular recognition of antagonists. Comparisons with previous structures reveal a mechanism for antagonist-induced inactivation of Cys-loop receptors, involving an expansion of the orthosteric binding site in the extracellular domain that is coupled to closure of the ion pore in the transmembrane domain. Crystal structure of human glycine receptor-alpha3 bound to antagonist strychnine.,Huang X, Chen H, Michelsen K, Schneider S, Shaffer PL Nature. 2015 Oct 8;526(7572):277-80. doi: 10.1038/nature14972. Epub 2015 Sep 28. PMID:26416729[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||