1eq8: Difference between revisions
New page: left|200px<br /><applet load="1eq8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eq8" /> '''THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERI... |
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[[Image:1eq8.gif|left|200px]]<br /><applet load="1eq8" size=" | [[Image:1eq8.gif|left|200px]]<br /><applet load="1eq8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT'''<br /> | ||
==Overview== | ==Overview== | ||
The structures of functional peptides corresponding to the predicted | 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== | ==About this Structure== | ||
1EQ8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica] with OH as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1EQ8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica] with <scene name='pdbligand=OH:'>OH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ8 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
[[Category: Gesell, J | [[Category: Gesell, J J.]] | ||
[[Category: Kim, Y.]] | [[Category: Kim, Y.]] | ||
[[Category: Marassi, F | [[Category: Marassi, F M.]] | ||
[[Category: Montal, M.]] | [[Category: Montal, M.]] | ||
[[Category: Oblatt-Montal, M.]] | [[Category: Oblatt-Montal, M.]] | ||
[[Category: Opella, S | [[Category: Opella, S J.]] | ||
[[Category: Valente, A | [[Category: Valente, A P.]] | ||
[[Category: OH]] | [[Category: OH]] | ||
[[Category: helical bundle]] | [[Category: helical bundle]] | ||
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[[Category: pentameric bundle]] | [[Category: pentameric bundle]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:24 2008'' | ||
Revision as of 13:30, 21 February 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 with as ligand. 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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