1n9p
From Proteopedia
(New page: 200px<br /><applet load="1n9p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n9p, resolution 1.80Å" /> '''Crystal Structure of...) |
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caption="1n9p, resolution 1.80Å" /> | caption="1n9p, resolution 1.80Å" /> | ||
'''Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1'''<br /> | '''Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Inward rectifier K(+) channels govern the resting membrane voltage in many | + | 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== | ==About this Structure== | ||
| - | 1N9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1N9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: potassium channel]] | [[Category: potassium channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:44 2008'' |
Revision as of 12:03, 21 February 2008
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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
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