2ih3

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(New page: 200px<br /><applet load="2ih3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ih3, resolution 1.72&Aring;" /> '''Ion selectivity in a...)
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[[Image:2ih3.gif|left|200px]]<br /><applet load="2ih3" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ih3.gif|left|200px]]<br /><applet load="2ih3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ih3, resolution 1.72&Aring;" />
caption="2ih3, resolution 1.72&Aring;" />
'''Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation'''<br />
'''Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation'''<br />
==Overview==
==Overview==
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Potassium channels are K+-selective protein pores in cell membrane. The, selectivity filter is the functional unit that allows K+ channels to, distinguish potassium (K+) and sodium (Na+) ions. The filter's structure, depends on whether K+ or Na+ ions are bound inside it. We synthesized a K+, channel containing the d-enantiomer of alanine in place of a conserved, glycine and found by x-ray crystallography that its filter maintains the, K+ (conductive) structure in the presence of Na+ and very low, concentrations of K+. This channel conducts Na+ in the absence of K+ but, not in the presence of K+. These findings demonstrate that the ability of, the channel to adapt its structure differently to K+ and Na+ is a, fundamental aspect of ion selectivity, as is the ability of multiple K+, ions to compete effectively with Na+ for the conductive filter.
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Potassium channels are K+-selective protein pores in cell membrane. The selectivity filter is the functional unit that allows K+ channels to distinguish potassium (K+) and sodium (Na+) ions. The filter's structure depends on whether K+ or Na+ ions are bound inside it. We synthesized a K+ channel containing the d-enantiomer of alanine in place of a conserved glycine and found by x-ray crystallography that its filter maintains the K+ (conductive) structure in the presence of Na+ and very low concentrations of K+. This channel conducts Na+ in the absence of K+ but not in the presence of K+. These findings demonstrate that the ability of the channel to adapt its structure differently to K+ and Na+ is a fundamental aspect of ion selectivity, as is the ability of multiple K+ ions to compete effectively with Na+ for the conductive filter.
==About this Structure==
==About this Structure==
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2IH3 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 K and 1EM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IH3 OCA].
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2IH3 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=K:'>K</scene> and <scene name='pdbligand=1EM:'>1EM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IH3 OCA].
==Reference==
==Reference==
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[[Category: Leonetti, M.]]
[[Category: Leonetti, M.]]
[[Category: MacKinnon, R.]]
[[Category: MacKinnon, R.]]
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[[Category: Muir, T.W.]]
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[[Category: Muir, T W.]]
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[[Category: Valiyaveetil, F.I.]]
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[[Category: Valiyaveetil, F I.]]
[[Category: 1EM]]
[[Category: 1EM]]
[[Category: K]]
[[Category: K]]
[[Category: ion channel d-amino acid semi-synthetic]]
[[Category: ion channel d-amino acid semi-synthetic]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:18:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:36 2008''

Revision as of 15:52, 21 February 2008


2ih3, resolution 1.72Å

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Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation

Overview

Potassium channels are K+-selective protein pores in cell membrane. The selectivity filter is the functional unit that allows K+ channels to distinguish potassium (K+) and sodium (Na+) ions. The filter's structure depends on whether K+ or Na+ ions are bound inside it. We synthesized a K+ channel containing the d-enantiomer of alanine in place of a conserved glycine and found by x-ray crystallography that its filter maintains the K+ (conductive) structure in the presence of Na+ and very low concentrations of K+. This channel conducts Na+ in the absence of K+ but not in the presence of K+. These findings demonstrate that the ability of the channel to adapt its structure differently to K+ and Na+ is a fundamental aspect of ion selectivity, as is the ability of multiple K+ ions to compete effectively with Na+ for the conductive filter.

About this Structure

2IH3 is a Single protein structure of sequence from Mus musculus and Streptomyces lividans with and as ligands. Full crystallographic information is available from OCA.

Reference

Ion selectivity in a semisynthetic K+ channel locked in the conductive conformation., Valiyaveetil FI, Leonetti M, Muir TW, Mackinnon R, Science. 2006 Nov 10;314(5801):1004-7. PMID:17095703

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