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1oed

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Revision as of 02:08, 12 September 2015

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

Structural highlights

1oed is a 5 chain structure with sequence from Torpedo marmorata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1abt, 1dxz, 1idg, 1idh, 1lk1, 1lxg, 1lxh, 1tor, 1tos, 3mra, 1eq8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ACHG_TORCA] 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. [ACHA_TORCA] 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. [ACHD_TORCA] 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. [ACHB_TORCA] 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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The nicotinic acetylcholine receptor controls electrical signalling between nerve and muscle cells by opening and closing a gated, membrane-spanning pore. Here we present an atomic model of the closed pore, obtained by electron microscopy of crystalline postsynaptic membranes. The pore is shaped by an inner ring of 5 alpha-helices, which curve radially to create a tapering path for the ions, and an outer ring of 15 alpha-helices, which coil around each other and shield the inner ring from the lipids. The gate is a constricting hydrophobic girdle at the middle of the lipid bilayer, formed by weak interactions between neighbouring inner helices. When acetylcholine enters the ligand-binding domain, it triggers rotations of the protein chains on opposite sides of the entrance to the pore. These rotations are communicated through the inner helices, and open the pore by breaking the girdle apart.

Structure and gating mechanism of the acetylcholine receptor pore.,Miyazawa A, Fujiyoshi Y, Unwin N Nature. 2003 Jun 26;423(6943):949-55. PMID:12827192^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Miyazawa A, Fujiyoshi Y, Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature. 2003 Jun 26;423(6943):949-55. PMID:12827192 doi:10.1038/nature01748

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oed"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1oed]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OED FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1abt|1abt]], [[1dxz|1dxz]], [[1idg|1idg]], [[1idh|1idh]], [[1lk1|1lk1]], [[1lxg|1lxg]], [[1lxh|1lxh]], [[1tor|1tor]], [[1tos|1tos]], [[3mra|3mra]], [[1eq8|1eq8]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oed OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oed RCSB], [http://www.ebi.ac.uk/pdbsum/1oed PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oed OCA], [http://pdbe.org/1oed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oed RCSB], [http://www.ebi.ac.uk/pdbsum/1oed PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1oed" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Ion channels|Ion channels]]
+*[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptor]]
 == References ==
 <references/>

1oed

From Proteopedia

Revision as of 02:08, 12 September 2015

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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