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2nr1

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[[Image:2nr1.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nr1 OCA], [http://www.ebi.ac.uk/pdbsum/2nr1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nr1 RCSB]</span>
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'''TRANSMEMBRANE SEGMENT 2 OF NMDA RECEPTOR NR1, NMR, 10 STRUCTURES'''
'''TRANSMEMBRANE SEGMENT 2 OF NMDA RECEPTOR NR1, NMR, 10 STRUCTURES'''
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[[Category: Opella, S.]]
[[Category: Opella, S.]]
[[Category: Sun, W.]]
[[Category: Sun, W.]]
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[[Category: m2]]
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[[Category: M2]]
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[[Category: nr1]]
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[[Category: Nr1]]
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[[Category: postsynaptic membrane]]
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[[Category: Postsynaptic membrane]]
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[[Category: receptor]]
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[[Category: Receptor]]
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[[Category: signal]]
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[[Category: Signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:48:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:07:05 2008''
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Revision as of 06:48, 4 May 2008

Image:2nr1.gif

Template:STRUCTURE 2nr1

TRANSMEMBRANE SEGMENT 2 OF NMDA RECEPTOR NR1, NMR, 10 STRUCTURES


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

2NR1 is a Single protein structure of sequence from Homo sapiens. 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 Sun May 4 09:48:19 2008

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