2itd

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[[Image:2itd.gif|left|200px]]
[[Image:2itd.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2itd |SIZE=350|CAPTION= <scene name='initialview01'>2itd</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_2itd", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BA:BARIUM+ION'>BA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= kcsA, skc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans])
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-->
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|DOMAIN=
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{{STRUCTURE_2itd| PDB=2itd | SCENE= }}
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|RELATEDENTRY=[[2itc|2ITC]], [[2itd|2ITD]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2itd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2itd OCA], [http://www.ebi.ac.uk/pdbsum/2itd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2itd RCSB]</span>
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}}
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'''Potassium Channel KcsA-Fab complex in Barium Chloride'''
'''Potassium Channel KcsA-Fab complex in Barium Chloride'''
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[[Category: Zhou, M.]]
[[Category: Zhou, M.]]
[[Category: 3d-structure]]
[[Category: 3d-structure]]
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[[Category: ion transport]]
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[[Category: Ion transport]]
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[[Category: ionic channel]]
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[[Category: Ionic channel]]
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[[Category: k channel]]
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[[Category: K channel]]
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[[Category: protein-antibody fab complex]]
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[[Category: Protein-antibody fab complex]]
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[[Category: transmembrane]]
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[[Category: Transmembrane]]
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[[Category: voltage-gated channel]]
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[[Category: Voltage-gated channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:51:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:48:17 2008''
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Revision as of 04:51, 4 May 2008

Image:2itd.gif

Template:STRUCTURE 2itd

Potassium Channel KcsA-Fab complex in Barium 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

2ITD is a Single protein structure of sequence from Mus musculus and Streptomyces lividans. 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 Page seeded by OCA on Sun May 4 07:51:09 2008

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