1eq8: Difference between revisions

[[Image:1eq8.gif|left|200px]]

'''THREE-DIMENSIONAL STRUCTURE OF THE PENTAMERIC HELICAL BUNDLE OF THE ACETYLCHOLINE RECEPTOR M2 TRANSMEMBRANE SEGMENT'''

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.

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].  

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:24:05 2008''