1eq8
From Proteopedia
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|PDB= 1eq8 |SIZE=350|CAPTION= <scene name='initialview01'>1eq8</scene> | |PDB= 1eq8 |SIZE=350|CAPTION= <scene name='initialview01'>1eq8</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=OH:HYDROXIDE ION'>OH</scene> | + | |LIGAND= <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1a11|1A11]], [[1cek|1CEK]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq8 OCA], [http://www.ebi.ac.uk/pdbsum/1eq8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eq8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Opella, S J.]] | [[Category: Opella, S J.]] | ||
[[Category: Valente, A P.]] | [[Category: Valente, A P.]] | ||
| - | [[Category: OH]] | ||
[[Category: helical bundle]] | [[Category: helical bundle]] | ||
[[Category: ion-channel]] | [[Category: ion-channel]] | ||
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[[Category: pentameric bundle]] | [[Category: pentameric bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:07:41 2008'' |
Revision as of 17:07, 30 March 2008
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| Ligands: | |||||||
| Related: | 1A11, 1CEK
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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