1eq8
From Proteopedia
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| - | [[Image:1eq8.gif|left|200px]] | + | [[Image:1eq8.gif|left|200px]] |
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| - | '''THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT''' | + | {{Structure |
| + | |PDB= 1eq8 |SIZE=350|CAPTION= <scene name='initialview01'>1eq8</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=OH:HYDROXIDE ION'>OH</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EQ8 is a [ | + | 1EQ8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ8 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: Single protein]] | [[Category: Single protein]] | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
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[[Category: helical bundle]] | [[Category: helical bundle]] | ||
[[Category: ion-channel]] | [[Category: ion-channel]] | ||
| - | [[Category: lipid | + | [[Category: lipid bilayer]] |
[[Category: m2]] | [[Category: m2]] | ||
[[Category: neurotransmitter receptor]] | [[Category: neurotransmitter receptor]] | ||
[[Category: pentameric bundle]] | [[Category: pentameric bundle]] | ||
| - | ''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 10:59:03 2008'' |
Revision as of 08:59, 20 March 2008
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THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT
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
1EQ8 is a Single protein structure of sequence from Torpedo californica. 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 10:59:03 2008
