1k4c: Difference between revisions
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|PDB= 1k4c |SIZE=350|CAPTION= <scene name='initialview01'>1k4c</scene>, resolution 2.00Å | |PDB= 1k4c |SIZE=350|CAPTION= <scene name='initialview01'>1k4c</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k4c OCA], [http://www.ebi.ac.uk/pdbsum/1k4c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k4c RCSB]</span> | |||
}} | }} | ||
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[[Category: Morais-Cabral, J H.]] | [[Category: Morais-Cabral, J H.]] | ||
[[Category: Zhou, Y.]] | [[Category: Zhou, Y.]] | ||
[[Category: k channel]] | [[Category: k channel]] | ||
[[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 Sun Mar 30 21:43:13 2008'' | ||
Revision as of 21:43, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Potassium Channel KcsA-Fab complex in high 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
1K4C is a Single protein structure of sequence from Mus musculus and Streptomyces lividans. The following page contains interesting information on the relation of 1K4C with [Potassium Channels]. 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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