2itc
From Proteopedia
(New page: 200px<br /> <applet load="2itc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2itc, resolution 3.200Å" /> '''Potassium Channel ...) |
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| - | [[Image:2itc.gif|left|200px]]<br /> | + | [[Image:2itc.gif|left|200px]]<br /><applet load="2itc" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2itc, resolution 3.200Å" /> | caption="2itc, resolution 3.200Å" /> | ||
'''Potassium Channel KcsA-Fab complex in Sodium Chloride'''<br /> | '''Potassium Channel KcsA-Fab complex in Sodium Chloride'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2ITC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2ITC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ITC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: voltage-gated channel]] | [[Category: voltage-gated channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:16:26 2008'' |
Revision as of 13:16, 23 January 2008
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Potassium Channel KcsA-Fab complex in Sodium Chloride
Overview
Thermodynamic measurements of ion binding to the Streptomyces lividans, K(+) channel were carried out using isothermal titration calorimetry, whereas atomic structures of ion-bound and ion-free conformations of the, channel were characterized by x-ray crystallography. Here we use these, assays to show that the ion radius dependence of selectivity stems from, the channel's recognition of ion size (i.e., volume) rather than charge, density. Ion size recognition is a function of the channel's ability to, adopt a very specific conductive structure with larger ions (K(+), Rb(+), Cs(+), and Ba(2+)) bound and not with smaller ions (Na(+), Mg(2+), and, Ca(2+)). The formation of the conductive structure involves selectivity, filter atoms that are in direct contact with bound ions as well as protein, atoms surrounding the selectivity filter up to a distance of 15 A from the, ions. We conclude that ion selectivity in a K(+) channel is a property of, size-matched ion binding sites created by the protein structure.
About this Structure
2ITC is a Single protein structure of sequence from Mus musculus and Streptomyces lividans with as ligand. Full crystallographic information is available from OCA.
Reference
Structural and thermodynamic properties of selective ion binding in a K+ channel., Lockless SW, Zhou M, MacKinnon R, PLoS Biol. 2007 May;5(5):e121. PMID:17472437
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