1n9p

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[[Image:1n9p.jpg|left|200px]]
[[Image:1n9p.jpg|left|200px]]
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{{Structure
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|PDB= 1n9p |SIZE=350|CAPTION= <scene name='initialview01'>1n9p</scene>, resolution 1.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1n9p", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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|GENE= GIRK1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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{{STRUCTURE_1n9p| PDB=1n9p | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9p OCA], [http://www.ebi.ac.uk/pdbsum/1n9p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n9p RCSB]</span>
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'''Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1'''
'''Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1'''
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[[Category: MacKinnon, R.]]
[[Category: MacKinnon, R.]]
[[Category: Nishida, M.]]
[[Category: Nishida, M.]]
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[[Category: beta barrel]]
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[[Category: Beta barrel]]
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[[Category: cytoplasmic domain]]
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[[Category: Cytoplasmic domain]]
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[[Category: g protein]]
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[[Category: G protein]]
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[[Category: inward rectifier]]
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[[Category: Inward rectifier]]
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[[Category: potassium channel]]
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[[Category: Potassium channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:16:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:27:24 2008''
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Revision as of 23:16, 2 May 2008

Template:STRUCTURE 1n9p

Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1


Overview

Inward rectifier K(+) channels govern the resting membrane voltage in many cells. Regulation of these ion channels via G protein-coupled receptor signaling underlies the control of heart rate and the actions of neurotransmitters in the central nervous system. We have determined the protein structure formed by the intracellular N- and C termini of the G protein-gated inward rectifier K(+) channel GIRK1 at 1.8 A resolution. A cytoplasmic pore, conserved among inward rectifier K(+) channels, extends the ion pathway to 60 A, nearly twice the length of a canonical transmembrane K(+) channel. The cytoplasmic pore is lined by acidic and hydrophobic amino acids, creating a favorable environment for polyamines, which block the pore. These results explain in structural and chemical terms the basis of inward rectification, and they also have implications for G protein regulation of GIRK channels.

About this Structure

1N9P is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution., Nishida M, MacKinnon R, Cell. 2002 Dec 27;111(7):957-65. PMID:12507423 Page seeded by OCA on Sat May 3 02:16:17 2008

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