1lnq
From Proteopedia
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'''CRYSTAL STRUCTURE OF MTHK AT 3.3 A''' | '''CRYSTAL STRUCTURE OF MTHK AT 3.3 A''' | ||
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[[Category: Lee, A.]] | [[Category: Lee, A.]] | ||
[[Category: Mackinnon, R.]] | [[Category: Mackinnon, R.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:05:39 2008'' | |
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Revision as of 21:05, 2 May 2008
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. 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 Sat May 3 00:05:39 2008
