1lnq
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| , resolution 3.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | mth1520 (Methanothermobacter thermautotrophicus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MTHK AT 3.3 A
OverviewOverview
Ion channels exhibit two essential biophysical properties; that is, selective ion conduction, and the ability to gate-open in response to an appropriate stimulus. Two general categories of ion channel gating are defined by the initiating stimulus: ligand binding (neurotransmitter- or second-messenger-gated channels) or membrane voltage (voltage-gated channels). Here we present the structural basis of ligand gating in a K(+) channel that opens in response to intracellular Ca(2+). We have cloned, expressed, analysed electrical properties, and determined the crystal structure of a K(+) channel (MthK) from Methanobacterium thermoautotrophicum in the Ca(2+)-bound, opened state. Eight RCK domains (regulators of K(+) conductance) form a gating ring at the intracellular membrane surface. The gating ring uses the free energy of Ca(2+) binding in a simple manner to perform mechanical work to open the pore.
About this StructureAbout this Structure
1LNQ is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. The following page contains interesting information on the relation of 1LNQ with [Potassium Channels]. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and mechanism of a calcium-gated potassium channel., Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R, Nature. 2002 May 30;417(6888):515-22. PMID:12037559
Page seeded by OCA on Sun Mar 30 22:05:01 2008