1k4d: Difference between revisions
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==Overview== | ==Overview== | ||
Ion transport proteins must remove an ion's hydration shell to coordinate | Ion transport proteins must remove an ion's hydration shell to coordinate the ion selectively on the basis of its size and charge. To discover how the K+ channel solves this fundamental aspect of ion conduction, we solved the structure of the KcsA K+ channel in complex with a monoclonal Fab antibody fragment at 2.0 A resolution. Here we show how the K+ channel displaces water molecules around an ion at its extracellular entryway, and how it holds a K+ ion in a square antiprism of water molecules in a cavity near its intracellular entryway. Carbonyl oxygen atoms within the selectivity filter form a very similar square antiprism around each K+ binding site, as if to mimic the waters of hydration. The selectivity filter changes its ion coordination structure in low K+ solutions. This structural change is crucial to the operation of the selectivity filter in the cellular context, where the K+ ion concentration near the selectivity filter varies in response to channel gating. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Kaufman, A.]] | [[Category: Kaufman, A.]] | ||
[[Category: MacKinnon, R.]] | [[Category: MacKinnon, R.]] | ||
[[Category: Morais-Cabral, J | [[Category: Morais-Cabral, J H.]] | ||
[[Category: Zhou, Y.]] | [[Category: Zhou, Y.]] | ||
[[Category: DGA]] | [[Category: DGA]] | ||
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[[Category: protein-antibody fab complex]] | [[Category: protein-antibody fab complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:00 2008'' | ||
Revision as of 14:30, 21 February 2008
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Potassium Channel KcsA-Fab complex in low concentration of K+
OverviewOverview
Ion transport proteins must remove an ion's hydration shell to coordinate the ion selectively on the basis of its size and charge. To discover how the K+ channel solves this fundamental aspect of ion conduction, we solved the structure of the KcsA K+ channel in complex with a monoclonal Fab antibody fragment at 2.0 A resolution. Here we show how the K+ channel displaces water molecules around an ion at its extracellular entryway, and how it holds a K+ ion in a square antiprism of water molecules in a cavity near its intracellular entryway. Carbonyl oxygen atoms within the selectivity filter form a very similar square antiprism around each K+ binding site, as if to mimic the waters of hydration. The selectivity filter changes its ion coordination structure in low K+ solutions. This structural change is crucial to the operation of the selectivity filter in the cellular context, where the K+ ion concentration near the selectivity filter varies in response to channel gating.
About this StructureAbout this Structure
1K4D is a Single protein structure of sequence from Mus musculus and Streptomyces lividans with , , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution., Zhou Y, Morais-Cabral JH, Kaufman A, MacKinnon R, Nature. 2001 Nov 1;414(6859):43-8. PMID:11689936
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