2gix
From Proteopedia
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|PDB= 2gix |SIZE=350|CAPTION= <scene name='initialview01'>2gix</scene>, resolution 2.020Å | |PDB= 2gix |SIZE=350|CAPTION= <scene name='initialview01'>2gix</scene>, resolution 2.020Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> | + | |LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Kcnj2, Irk1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Kcnj2, Irk1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gix OCA], [http://www.ebi.ac.uk/pdbsum/2gix PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gix RCSB]</span> | ||
}} | }} | ||
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[[Category: Pegan, S.]] | [[Category: Pegan, S.]] | ||
[[Category: Slesinger, P A.]] | [[Category: Slesinger, P A.]] | ||
| - | [[Category: K]] | ||
| - | [[Category: MPD]] | ||
[[Category: andersen's mutation]] | [[Category: andersen's mutation]] | ||
[[Category: cytoplasmic domains of kir2 1]] | [[Category: cytoplasmic domains of kir2 1]] | ||
| - | ''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 03:17:14 2008'' |
Revision as of 00:17, 31 March 2008
| |||||||
| , resolution 2.020Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | Kcnj2, Irk1 (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Cytoplasmic Domain Structure of Kir2.1 containing Andersen's Mutation R218Q and Rescue Mutation T309K
Overview
Kir2.1 channels play a key role in maintaining the correct resting potential in eukaryotic cells. Recently, specific amino acid mutations in the Kir2.1 inwardly rectifying potassium channel have been found to cause Andersen's Syndrome in humans. Here, we have characterized individual Andersen's Syndrome mutants R218Q, G300V, E303K, and delta314-315 and have found multiple effects on the ability of the cytoplasmic domains in Kir2.1 channels to form proper tetrameric assemblies. For the R218Q mutation, we identified a second site mutation (T309K) that restored tetrameric assembly but not function. We successfully crystallized and solved the structure (at 2.0 A) of the N- and C-terminal cytoplasmic domains of Kir2.1-R218Q/T309K(S). This new structure revealed multiple conformations of the G-loop and CD loop, providing an explanation for channels that assemble but do not conduct ions. Interestingly, Glu303 forms both intra- and intersubunit salt bridges, depending on the conformation of the G-loop, suggesting that the E303K mutant stabilizes both closed and open G-loop conformations. In the Kir2.1-R218Q/T309K(S) structure, we discovered that the DE loop forms a hydrophobic pocket that binds 2-methyl-2,4-pentanediol, which is located near the putative G(betagamma)-activation site of Kir3 channels. Finally, we observed a potassium ion bound to the cytoplasmic domain for this class of K+ channels.
About this Structure
2GIX is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1., Pegan S, Arrabit C, Slesinger PA, Choe S, Biochemistry. 2006 Jul 18;45(28):8599-606. PMID:16834334
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