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Role of the C-terminal domain in the structure and function of tetrameric sodium channels
DOI:
10.1038/ncomms3465
PMID:
24051986
Authors:
Claire
Bagneris
(Birkbeck, University of London)
,
Paul G.
Decaen
(Howard Hughes Medical Institute; Harvard Medical School)
,
Benjamin A.
Hall
(Microsoft Research Cambridge)
,
Claire E.
Naylor
(Birkbeck, University of London)
,
David E.
Clapham
(Howard Hughes Medical Institute, Children’s Hospital Boston)
,
Christopher W. M.
Kay
(Howard Hughes Medical Institute; Harvard Medical School)
,
B. A.
Wallace
(Birkbeck, University of London)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Nature Communications
, VOL 4
, PAGES 7195-7197
State:
Published (Approved)
Published:
September 2013

Abstract: Voltage-gated sodium channels have essential roles in electrical signalling. Prokaryotic sodium channels are tetramers consisting of transmembrane (TM) voltage-sensing and pore domains, and a cytoplasmic carboxy-terminal domain. Previous crystal structures of bacterial sodium channels revealed the nature of their TM domains but not their C-terminal domains (CTDs). Here, using electron paramagnetic resonance (EPR) spectroscopy combined with molecular dynamics, we show that the CTD of the NavMs channel from Magnetococcus marinus includes a flexible region linking the TM domains to a four-helix coiled-coil bundle.
Journal Keywords: Amino; Bacterial; Crystallography; X-Ray; Electron; Escherichia; Ion;Protein; Secondary; Protein; Tertiary; Recombinant; Static; Voltage-Gated Sodium Channels
Subject Areas:
Biology and Bio-materials
Diamond Offline Facilities:
Membrane Protein Laboratory (MPL)
Instruments:
I02-Macromolecular Crystallography
,
I04-Macromolecular Crystallography
Other Facilities: Soleil, France (beamline Proxima 1)
Added On:
24/09/2013 10:56
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