2nlj: Difference between revisions

Revision as of 15:38, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nlj.png

Template:STRUCTURE 2nlj

Potassium Channel KcsA(M96V)-Fab complex in KClPotassium Channel KcsA(M96V)-Fab complex in KCl

Template:ABSTRACT PUBMED 17472437

About this StructureAbout this Structure

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

ReferenceReference

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 Jul 27 15:38:36 2008

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OCA

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+===Potassium Channel KcsA(M96V)-Fab complex in KCl===
-==Overview==
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-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.
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 [[Category: Transmembrane]]
 [[Category: Voltage-gated channel]]
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