1cek
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1cek.gif|left|200px]] | + | [[Image:1cek.gif|left|200px]] |
| - | + | ||
| - | '''THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY''' | + | {{Structure |
| + | |PDB= 1cek |SIZE=350|CAPTION= <scene name='initialview01'>1cek</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1CEK is a [ | + | 1CEK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEK OCA]. |
==Reference== | ==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:// | + | 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: Single protein]] | ||
| Line 22: | Line 31: | ||
[[Category: acetylcholine receptor]] | [[Category: acetylcholine receptor]] | ||
[[Category: ion-channel]] | [[Category: ion-channel]] | ||
| - | [[Category: lipid | + | [[Category: lipid bilayer]] |
[[Category: m2]] | [[Category: m2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:24 2008'' |
Revision as of 08:23, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY
Overview
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.
About this Structure
1CEK is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from 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:10201407
Page seeded by OCA on Thu Mar 20 10:23:24 2008
