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1cek
From Proteopedia
(New page: 200px<br /><applet load="1cek" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cek" /> '''THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-...) |
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| - | [[Image:1cek.gif|left|200px]]<br /><applet load="1cek" size=" | + | [[Image:1cek.gif|left|200px]]<br /><applet load="1cek" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cek" /> | caption="1cek" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY'''<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== | ||
| - | 1CEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1CEK is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[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: acetylcholine receptor]] | [[Category: acetylcholine receptor]] | ||
[[Category: ion-channel]] | [[Category: ion-channel]] | ||
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[[Category: m2]] | [[Category: m2]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:16 2008'' |
Revision as of 10:05, 21 February 2008
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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
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