1eq8: Difference between revisions
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[[Image:1eq8.gif|left|200px]] | [[Image:1eq8.gif|left|200px]] | ||
'''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''' | |||
==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]] | ||
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Revision as of 11:59, 20 March 2008
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THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT
OverviewOverview
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 StructureAbout this Structure
1EQ8 is a Single protein structure of sequence from Torpedo californica. Full crystallographic information is available from OCA.
ReferenceReference
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
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