8v86
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8v86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8v86 OCA], [https://pdbe.org/8v86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8v86 RCSB], [https://www.ebi.ac.uk/pdbsum/8v86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8v86 ProSAT]</span></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=8v86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8v86 OCA], [https://pdbe.org/8v86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8v86 RCSB], [https://www.ebi.ac.uk/pdbsum/8v86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8v86 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | = | + | <div style="background-color:#fffaf0;"> |
| - | + | == Publication Abstract from PubMed == | |
| - | == | + | The alpha7 nicotinic acetylcholine receptor is a pentameric ligand-gated ion channel that plays an important role in cholinergic signaling throughout the nervous system. Its unique physiological characteristics and implications in neurological disorders and inflammation make it a promising but challenging therapeutic target. Positive allosteric modulators overcome limitations of traditional alpha7 agonists, but their potentiation mechanisms remain unclear. Here, we present high-resolution structures of alpha7-modulator complexes, revealing partially overlapping binding sites but varying conformational states. Structure-guided functional and computational tests suggest that differences in modulator activity arise from the stable rotation of a channel gating residue out of the pore. We extend the study using a time-resolved cryoelectron microscopy (cryo-EM) approach to reveal asymmetric state transitions for this homomeric channel and also find that a modulator with allosteric agonist activity exploits a distinct channel-gating mechanism. These results define mechanisms of alpha7 allosteric modulation and activation with implications across the pentameric receptor superfamily. |
| - | + | ||
| + | , PMID:38382524<ref>PMID:38382524</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8v86" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Alpha7-nicotinic acetylcholine receptor bound to GAT107
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