7koq: Difference between revisions
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Alpha-7 nicotinic acetylcholine receptor bound to epibatidine in a desensitized state== | ||
<StructureSection load='7koq' size='340' side='right'caption='[[7koq]], [[Resolution|resolution]] 3.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7koq]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KOQ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPJ:EPIBATIDINE'>EPJ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHRNA7, NACHRA7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=7koq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7koq OCA], [https://pdbe.org/7koq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7koq RCSB], [https://www.ebi.ac.uk/pdbsum/7koq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7koq ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[https://www.uniprot.org/uniprot/ACHA7_HUMAN ACHA7_HUMAN]] 15q13.3 microdeletion syndrome. | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/ACHA7_HUMAN ACHA7_HUMAN]] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The alpha7 nicotinic acetylcholine receptor plays critical roles in the central nervous system and in the cholinergic inflammatory pathway. This ligand-gated ion channel assembles as a homopentamer, is exceptionally permeable to Ca(2+), and desensitizes faster than any other Cys-loop receptor. The alpha7 receptor has served as a prototype for the Cys-loop superfamily yet has proven refractory to structural analysis. We present cryo-EM structures of the human alpha7 nicotinic receptor in a lipidic environment in resting, activated, and desensitized states, illuminating the principal steps in the gating cycle. The structures also reveal elements that contribute to its function, including a C-terminal latch that is permissive for channel opening, and an anionic ring in the extracellular vestibule that contributes to its high conductance and calcium permeability. Comparisons among the alpha7 structures provide a foundation for mapping the gating cycle and reveal divergence in gating mechanisms in the Cys-loop receptor superfamily. | |||
Structure and gating mechanism of the alpha7 nicotinic acetylcholine receptor.,Noviello CM, Gharpure A, Mukhtasimova N, Cabuco R, Baxter L, Borek D, Sine SM, Hibbs RE Cell. 2021 Mar 11. pii: S0092-8674(21)00238-5. doi: 10.1016/j.cell.2021.02.049. PMID:33735609<ref>PMID:33735609</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7koq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Large Structures]] | |||
[[Category: Baxter, L]] | |||
[[Category: Borek, D]] | |||
[[Category: Cabuco, R]] | |||
[[Category: Gharpure, A]] | |||
[[Category: Hibbs, R E]] | |||
[[Category: Mukhtasimova, N]] | |||
[[Category: Noviello, C M]] | |||
[[Category: Sine, S]] | |||
[[Category: Cys-loop receptor]] | |||
[[Category: Membrane protein]] | |||
Latest revision as of 13:51, 31 March 2021
Alpha-7 nicotinic acetylcholine receptor bound to epibatidine in a desensitized stateAlpha-7 nicotinic acetylcholine receptor bound to epibatidine in a desensitized state
Structural highlights
Disease[ACHA7_HUMAN] 15q13.3 microdeletion syndrome. Function[ACHA7_HUMAN] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin. Publication Abstract from PubMedThe alpha7 nicotinic acetylcholine receptor plays critical roles in the central nervous system and in the cholinergic inflammatory pathway. This ligand-gated ion channel assembles as a homopentamer, is exceptionally permeable to Ca(2+), and desensitizes faster than any other Cys-loop receptor. The alpha7 receptor has served as a prototype for the Cys-loop superfamily yet has proven refractory to structural analysis. We present cryo-EM structures of the human alpha7 nicotinic receptor in a lipidic environment in resting, activated, and desensitized states, illuminating the principal steps in the gating cycle. The structures also reveal elements that contribute to its function, including a C-terminal latch that is permissive for channel opening, and an anionic ring in the extracellular vestibule that contributes to its high conductance and calcium permeability. Comparisons among the alpha7 structures provide a foundation for mapping the gating cycle and reveal divergence in gating mechanisms in the Cys-loop receptor superfamily. Structure and gating mechanism of the alpha7 nicotinic acetylcholine receptor.,Noviello CM, Gharpure A, Mukhtasimova N, Cabuco R, Baxter L, Borek D, Sine SM, Hibbs RE Cell. 2021 Mar 11. pii: S0092-8674(21)00238-5. doi: 10.1016/j.cell.2021.02.049. PMID:33735609[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||