2bg9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:46, 23 October 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2bg9.png|left|200px]]
 
-
<!--
+
==REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.==
-
The line below this paragraph, containing "STRUCTURE_2bg9", creates the "Structure Box" on the page.
+
<SX load='2bg9' size='340' side='right' viewer='molstar' caption='[[2bg9]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2bg9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. The November 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Acetylcholine Receptor'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_11 10.2210/rcsb_pdb/mom_2005_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BG9 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</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=2bg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bg9 OCA], [https://pdbe.org/2bg9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bg9 RCSB], [https://www.ebi.ac.uk/pdbsum/2bg9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bg9 ProSAT]</span></td></tr>
-
{{STRUCTURE_2bg9| PDB=2bg9 | SCENE= }}
+
</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.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/2bg9_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bg9 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
We present a refined model of the membrane-associated Torpedo acetylcholine (ACh) receptor at 4A resolution. An improved experimental density map was obtained from 342 electron images of helical tubes, and the refined structure was derived to an R-factor of 36.7% (R(free) 37.9%) by standard crystallographic methods, after placing the densities corresponding to a single molecule into an artificial unit cell. The agreement between experimental and calculated phases along the helical layer-lines was used to monitor progress in the refinement and to give an independent measure of the accuracy. The atomic model allowed a detailed description of the whole receptor in the closed-channel form, including the ligand-binding and intracellular domains, which have not previously been interpreted at a chemical level. We confirm that the two ligand-binding alpha subunits have a different extended conformation from the three other subunits in the closed channel, and identify several interactions on both pairs of subunit interfaces, and within the alpha subunits, which may be responsible for their "distorted" structures. The ACh-coordinating amino acid side-chains of the alpha subunits are far apart in the closed channel, indicating that a localised rearrangement, involving closure of loops B and C around the bound ACh molecule, occurs upon activation. A comparison of the structure of the alpha subunit with that of AChBP having ligand present, suggests how the localised rearrangement overcomes the distortions and initiates the rotational movements associated with opening of the channel. Both vestibules of the channel are strongly electronegative, providing a cation-stabilising environment at either entrance of the membrane pore. Access to the pore on the intracellular side is further influenced by narrow lateral windows, which would be expected to screen out electrostatically ions of the wrong charge and size.
-
===REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.===
+
Refined structure of the nicotinic acetylcholine receptor at 4A resolution.,Unwin N J Mol Biol. 2005 Mar 4;346(4):967-89. Epub 2005 Jan 25. PMID:15701510<ref>PMID:15701510</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2bg9" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_15701510}}, adds the Publication Abstract to the page
+
*[[Acetyl choline receptor 3D structures|Acetyl choline receptor 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 15701510 is the PubMed ID number.
+
*[[Ionotropic receptors|Ionotropic receptors]]
-
-->
+
*[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptor]]
-
{{ABSTRACT_PUBMED_15701510}}
+
*[[5-hydroxytryptamine receptor|5-hydroxytryptamine receptor]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
2BG9 is a 5 chains structure with sequences from [http://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. The November 2005 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Acetylcholine Receptor'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_11 10.2210/rcsb_pdb/mom_2005_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BG9 OCA].
+
__TOC__
-
 
+
</SX>
-
==Reference==
+
-
<ref group="xtra">PMID:15701510</ref><ref group="xtra">PMID:12827192</ref><references group="xtra"/>
+
[[Category: Acetylcholine Receptor]]
[[Category: Acetylcholine Receptor]]
 +
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Torpedo marmorata]]
[[Category: Torpedo marmorata]]
-
[[Category: Unwin, N.]]
+
[[Category: Unwin N]]
-
[[Category: Acetylcholine receptor]]
+
-
[[Category: Electron microscopy]]
+
-
[[Category: Ion channel]]
+
-
[[Category: Ion channel/receptor]]
+
-
[[Category: Ion transport]]
+
-
[[Category: Postsynaptic membrane]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 21 09:44:48 2010''
+

Current revision

REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.

2bg9, resolution 4.00Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bg9"
Personal tools