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1lnq
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(New page: 200px<br /> <applet load="1lnq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lnq, resolution 3.30Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 06:56, 18 November 2007
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CRYSTAL STRUCTURE OF MTHK AT 3.3 A
Overview
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 Structure
1LNQ is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with CA as ligand. The following page contains interesting information on the relation of 1LNQ with [Potassium Channels]. Full crystallographic information is available from OCA.
Reference
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 Nov 18 09:03:20 2007
