2ih3: Difference between revisions
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|PDB= 2ih3 |SIZE=350|CAPTION= <scene name='initialview01'>2ih3</scene>, resolution 1.72Å | |PDB= 2ih3 |SIZE=350|CAPTION= <scene name='initialview01'>2ih3</scene>, resolution 1.72Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=1EM:(1S)-2-HYDROXY-1-[(NONANOYLOXY)METHYL]ETHYL+MYRISTATE'>1EM</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= kcsA, skc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans]) | |GENE= kcsA, skc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2ih1|2IH1]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ih3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ih3 OCA], [http://www.ebi.ac.uk/pdbsum/2ih3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ih3 RCSB]</span> | |||
}} | }} | ||
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[[Category: Muir, T W.]] | [[Category: Muir, T W.]] | ||
[[Category: Valiyaveetil, F I.]] | [[Category: Valiyaveetil, F I.]] | ||
[[Category: ion channel d-amino acid semi-synthetic]] | [[Category: ion channel d-amino acid semi-synthetic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:44:15 2008'' | ||
Revision as of 03:44, 31 March 2008
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| , resolution 1.72Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | kcsA, skc1 (Streptomyces lividans) | ||||||
| Related: | 2IH1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Ion selectivity in a semi-synthetic K+ channel locked in the conductive conformation
OverviewOverview
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 StructureAbout this Structure
2IH3 is a Single protein structure of sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA.
ReferenceReference
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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