3sq6: Difference between revisions
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==Crystal Structures of the Ligand Binding Domain of a Pentameric Alpha7 Nicotinic Receptor Chimera with its Agonist Epibatidine== | ==Crystal Structures of the Ligand Binding Domain of a Pentameric Alpha7 Nicotinic Receptor Chimera with its Agonist Epibatidine== | ||
<StructureSection load='3sq6' size='340' side='right' caption='[[3sq6]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3sq6' size='340' side='right'caption='[[3sq6]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3sq6]] is a 10 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3sq6]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Lymnaea_stagnalis Lymnaea stagnalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SQ6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPJ:EPIBATIDINE'>EPJ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3sq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sq6 OCA], [https://pdbe.org/3sq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sq6 RCSB], [https://www.ebi.ac.uk/pdbsum/3sq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sq6 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Acetylcholine binding protein|Acetylcholine binding protein]] | *[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Bren | [[Category: Large Structures]] | ||
[[Category: Chen | [[Category: Lymnaea stagnalis]] | ||
[[Category: Dellisanti | [[Category: Bren N]] | ||
[[Category: Huang | [[Category: Chen L]] | ||
[[Category: Li | [[Category: Dellisanti C]] | ||
[[Category: Noridomi | [[Category: Huang S]] | ||
[[Category: Sine | [[Category: Li S-X]] | ||
[[Category: Noridomi K]] | |||
[[Category: Sine S]] | |||
Latest revision as of 11:09, 9 October 2024
Crystal Structures of the Ligand Binding Domain of a Pentameric Alpha7 Nicotinic Receptor Chimera with its Agonist EpibatidineCrystal Structures of the Ligand Binding Domain of a Pentameric Alpha7 Nicotinic Receptor Chimera with its Agonist Epibatidine
Structural highlights
Publication Abstract from PubMedThe alpha(7) acetylcholine receptor (AChR) mediates pre- and postsynaptic neurotransmission in the central nervous system and is a potential therapeutic target in neurodegenerative, neuropsychiatric and inflammatory disorders. We determined the crystal structure of the extracellular domain of a receptor chimera constructed from the human alpha(7) AChR and Lymnaea stagnalis acetylcholine binding protein (AChBP), which shares 64% sequence identity and 71% similarity with native alpha(7). We also determined the structure with bound epibatidine, a potent AChR agonist. Comparison of the structures revealed molecular rearrangements and interactions that mediate agonist recognition and early steps in signal transduction in alpha(7) AChRs. The structures further revealed a ring of negative charge within the central vestibule, poised to contribute to cation selectivity. Structure-guided mutational studies disclosed distinctive contributions to agonist recognition and signal transduction in alpha(7) AChRs. The structures provide a realistic template for structure-aided drug design and for defining structure-function relationships of alpha(7) AChRs. Ligand-binding domain of an alpha7-nicotinic receptor chimera and its complex with agonist.,Li SX, Huang S, Bren N, Noridomi K, Dellisanti CD, Sine SM, Chen L Nat Neurosci. 2011 Sep 11;14(10):1253-9. doi: 10.1038/nn.2908. PMID:21909087[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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