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New page: '''Unreleased structure''' The entry 4bot is ON HOLD until Paper Publication Authors: Zuber, B., Unwin, N. Description: The structure and super-organization of acetylcholine receptor-r...
 
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'''Unreleased structure'''


The entry 4bot is ON HOLD  until Paper Publication
==The structure and super-organization of acetylcholine receptor- rapsyn complexes class E==
<SX load='4bot' size='340' side='right' viewer='molstar' caption='[[4bot]], [[Resolution|resolution]] 42.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bot]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BOT FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4bog|4bog]], [[4boi|4boi]], [[4bon|4bon]], [[4boo|4boo]], [[4bor|4bor]]</div></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=4bot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bot OCA], [https://pdbe.org/4bot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bot RCSB], [https://www.ebi.ac.uk/pdbsum/4bot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bot ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/ACHA_TORMA ACHA_TORMA]] 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.
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== Publication Abstract from PubMed ==
The scaffolding protein at the neuromuscular junction, rapsyn, enables clustering of nicotinic acetylcholine receptors in high concentration and is critical for muscle function. Patients with insufficient receptor clustering suffer from muscle weakness. However, the detailed organization of the receptor-rapsyn network is poorly understood: it is unclear whether rapsyn first forms a wide meshwork to which receptors can subsequently dock or whether it only forms short bridges linking receptors together to make a large cluster. Furthermore, the number of rapsyn-binding sites per receptor (a heteropentamer) has been controversial. Here, we show by cryoelectron tomography and subtomogram averaging of Torpedo postsynaptic membrane that receptors are connected by up to three rapsyn bridges, the minimum number required to form a 2D network. Half of the receptors belong to rapsyn-connected groups comprising between two and fourteen receptors. Our results provide a structural basis for explaining the stability and low diffusion of receptors within clusters.


Authors: Zuber, B., Unwin, N.
Structure and superorganization of acetylcholine receptor-rapsyn complexes.,Zuber B, Unwin N Proc Natl Acad Sci U S A. 2013 Jun 10. PMID:23754381<ref>PMID:23754381</ref>


Description: The structure and super-organization of acetylcholine receptor-rapsyn complexes class E
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4bot" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptor]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Torpedo marmorata]]
[[Category: Unwin, N]]
[[Category: Zuber, B]]
[[Category: Clustering]]
[[Category: Neuromuscular junction]]
[[Category: Neurotransmitter receptor]]
[[Category: Nicotinic]]
[[Category: Synapse]]
[[Category: Transport protein]]

Latest revision as of 10:20, 31 August 2022

The structure and super-organization of acetylcholine receptor- rapsyn complexes class EThe structure and super-organization of acetylcholine receptor- rapsyn complexes class E

4bot, resolution 42.00Å

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