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Title
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Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment.
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Authors
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S.B.Long,
X.Tao,
E.B.Campbell,
R.MacKinnon.
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Ref.
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Nature, 2007,
450,
376-382.
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PubMed id
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Abstract
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Voltage-dependent K+ (Kv) channels repolarize the action potential in neurons
and muscle. This type of channel is gated directly by membrane voltage through
protein domains known as voltage sensors, which are molecular voltmeters that
read the membrane voltage and regulate the pore. Here we describe the structure
of a chimaeric voltage-dependent K+ channel, which we call the 'paddle-chimaera
channel', in which the voltage-sensor paddle has been transferred from Kv2.1 to
Kv1.2. Crystallized in complex with lipids, the complete structure at 2.4
ångström resolution reveals the pore and voltage sensors embedded in a
membrane-like arrangement of lipid molecules. The detailed structure, which can
be compared directly to a large body of functional data, explains charge
stabilization within the membrane and suggests a mechanism for voltage-sensor
movements and pore gating.
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