1cek

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:39, 22 November 2023) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1cek.png|left|200px]]
 
-
<!--
+
==THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY==
-
The line below this paragraph, containing "STRUCTURE_1cek", creates the "Structure Box" on the page.
+
<StructureSection load='1cek' size='340' side='right'caption='[[1cek]]' 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'>[[1cek]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEK 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">Solid-state NMR</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=1cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cek OCA], [https://pdbe.org/1cek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cek RCSB], [https://www.ebi.ac.uk/pdbsum/1cek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cek ProSAT]</span></td></tr>
-
{{STRUCTURE_1cek| PDB=1cek | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ACHD_RAT ACHD_RAT] 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.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The structures of functional peptides corresponding to the predicted channel-lining M2 segments of the nicotinic acetylcholine receptor (AChR) and of a glutamate receptor of the NMDA subtype (NMDAR) were determined using solution NMR experiments on micelle samples, and solid-state NMR experiments on bilayer samples. Both M2 segments form straight transmembrane alpha-helices with no kinks. The AChR M2 peptide inserts in the lipid bilayer at an angle of 12 degrees relative to the bilayer normal, with a rotation about the helix long axis such that the polar residues face the N-terminal side of the membrane, which is assigned to be intracellular. A model built from these solid-state NMR data, and assuming a symmetric pentameric arrangement of M2 helices, results in a funnel-like architecture for the channel, with the wide opening on the N-terminal intracellular side.
-
===THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY===
+
Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy.,Opella SJ, Marassi FM, Gesell JJ, Valente AP, Kim Y, Oblatt-Montal M, Montal M Nat Struct Biol. 1999 Apr;6(4):374-9. PMID:10201407<ref>PMID:10201407</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_10201407}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1cek" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 10201407 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_10201407}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
1CEK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEK OCA].
+
-
 
+
-
==Reference==
+
-
Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy., Opella SJ, Marassi FM, Gesell JJ, Valente AP, Kim Y, Oblatt-Montal M, Montal M, Nat Struct Biol. 1999 Apr;6(4):374-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10201407 10201407]
+
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
-
[[Category: Single protein]]
+
[[Category: Gesell JJ]]
-
[[Category: Gesell, J J.]]
+
[[Category: Kim Y]]
-
[[Category: Kim, Y.]]
+
[[Category: Marassi FM]]
-
[[Category: Marassi, F M.]]
+
[[Category: Montal M]]
-
[[Category: Montal, M.]]
+
[[Category: Oblatt-Montal M]]
-
[[Category: Oblatt-Montal, M.]]
+
[[Category: Opella SJ]]
-
[[Category: Opella, S J.]]
+
[[Category: Valente AP]]
-
[[Category: Valente, A P.]]
+
-
[[Category: Acetylcholine receptor]]
+
-
[[Category: Ion-channel]]
+
-
[[Category: Lipid bilayer]]
+
-
[[Category: M2]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:38:17 2008''
+

Current revision

THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY

PDB ID 1cek

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cek"
Personal tools