ArticleBiophysical journal2010
Independent and cooperative motions of the Kv1.2 channel: voltage sensing and gating.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Structure-Encoded Global Motions and Their Role in Mediating Protein-Substrate Interactions.Biophysical journal · 2015Review
- Normal mode dynamics of voltage-gated K(+) channels: gating principle, opening mechanism, and inhibition.Journal of computational neuroscience · 2015Article
- Structure, dynamics and implied gating mechanism of a human cyclic nucleotide-gated channel.PLoS computational biology · 2014Article
- General rules for the arrangements and gating motions of pore-lining helices in homomeric ion channels.Nature communications · 2014Article
- Structural characterization of the voltage-sensor domain and voltage-gated K+-channel proteins vectorially oriented within a single bilayer membrane at the solid/vapor and solid/liquid interfaces via neutron interferometry.Langmuir : the ACS journal of surfaces and colloids · 2012Article
- Structure and flexibility of the C-ring in the electromotor of rotary F(0)F(1)-ATPase of pea chloroplasts.PloS one · 2012Article
- Profile structures of the voltage-sensor domain and the voltage-gated K(+)-channel vectorially oriented in a single phospholipid bilayer membrane at the solid-vapor and solid-liquid interfaces determined by x-ray interferometry.Physical review. E, Statistical, nonlinear, and soft matter physics · 2011Article
- Dynamic allostery: linkers are not merely flexible.Structure (London, England : 1993) · 2011Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Voltage-gated potassium (Kv) channels, such as Kv1.2, are involved in the generation and propagation of action potentials. The Kv channel is a homotetramer, and each monomer is composed of a voltage-sensing domain (VSD) and a pore domain (PD). We analyzed the fluctuations of a model structure of Kv1.2 using elastic network models. The analysis suggested a network of coupled fluctuations of eight rigid structural units and seven hinges that may control the transition between the active and inactive states of the channel. For the most part, the network is composed of amino acids that are known to affect channel activity. The results suggested allosteric interactions and cooperativity between the subunits in the coupling between the motion of the VSD and the selectivity filter of the PD, in accordance with recent empirical data. There are no direct contacts between the VSDs of the four subunits, and the contacts between these and the PDs are loose, suggesting that the VSDs are capable of functioning independently. Indeed, they manifest many inherent fluctuations that are decoupled from the rest of the structure. In general, the analysis suggests that the two domains contribute to the channel function both individually and cooperatively.
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