1zto: Difference between revisions
New page: left|200px<br /><applet load="1zto" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zto" /> '''INACTIVATION GATE OF POTASSIUM CHANNEL RCK4,... |
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[[Image:1zto.jpg|left|200px]]<br /><applet load="1zto" size=" | [[Image:1zto.jpg|left|200px]]<br /><applet load="1zto" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''INACTIVATION GATE OF POTASSIUM CHANNEL RCK4, NMR, 8 STRUCTURES'''<br /> | '''INACTIVATION GATE OF POTASSIUM CHANNEL RCK4, NMR, 8 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
The electrical signalling properties of neurons originate largely from the | The electrical signalling properties of neurons originate largely from the gating properties of their ion channels. N-type inactivation of voltage-gated potassium (Kv) channels is the best-understood gating transition in ion channels, and occurs by a 'ball-and-chain' type mechanism. In this mechanism an N-terminal domain (inactivation gate), which is tethered to the cytoplasmic side of the channel protein by a protease-cleavable chain, binds to its receptor at the inner vestibule of the channel, thereby physically blocking the pore. Even when synthesized as a peptide, ball domains restore inactivation in Kv channels whose inactivation domains have been deleted. Using high-resolution nuclear magnetic resonance (NMR) spectroscopy, we analysed the three-dimensional structure of the ball peptides from two rapidly inactivating mammalian K. channels (Raw3 (Kv3.4) and RCK4 (Kv1.4)). The inactivation peptide of Raw3 (Raw3-IP) has a compact structure that exposes two phosphorylation sites and allows the formation of an intramolecular disulphide bridge between two spatially close cysteine residues. Raw3-IP exhibits a characteristic surface charge pattern with a positively charged, a hydrophobic, and a negatively charged region. The RCK4 inactivation peptide (RCK4-IP) shows a similar spatial distribution of charged and uncharged regions, but is more flexible and less ordered in its amino-terminal part. | ||
==About this Structure== | ==About this Structure== | ||
1ZTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1ZTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZTO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Frank, R.]] | [[Category: Frank, R.]] | ||
[[Category: Geyer, M.]] | [[Category: Geyer, M.]] | ||
[[Category: Guy, H | [[Category: Guy, H R.]] | ||
[[Category: Kalbitzer, H | [[Category: Kalbitzer, H R.]] | ||
[[Category: Ruppersberg, J | [[Category: Ruppersberg, J P.]] | ||
[[Category: Schott, M.]] | [[Category: Schott, M.]] | ||
[[Category: inactivation gate]] | [[Category: inactivation gate]] | ||
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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 16:18:58 2008'' | ||
Revision as of 17:18, 21 February 2008
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INACTIVATION GATE OF POTASSIUM CHANNEL RCK4, NMR, 8 STRUCTURES
OverviewOverview
The electrical signalling properties of neurons originate largely from the gating properties of their ion channels. N-type inactivation of voltage-gated potassium (Kv) channels is the best-understood gating transition in ion channels, and occurs by a 'ball-and-chain' type mechanism. In this mechanism an N-terminal domain (inactivation gate), which is tethered to the cytoplasmic side of the channel protein by a protease-cleavable chain, binds to its receptor at the inner vestibule of the channel, thereby physically blocking the pore. Even when synthesized as a peptide, ball domains restore inactivation in Kv channels whose inactivation domains have been deleted. Using high-resolution nuclear magnetic resonance (NMR) spectroscopy, we analysed the three-dimensional structure of the ball peptides from two rapidly inactivating mammalian K. channels (Raw3 (Kv3.4) and RCK4 (Kv1.4)). The inactivation peptide of Raw3 (Raw3-IP) has a compact structure that exposes two phosphorylation sites and allows the formation of an intramolecular disulphide bridge between two spatially close cysteine residues. Raw3-IP exhibits a characteristic surface charge pattern with a positively charged, a hydrophobic, and a negatively charged region. The RCK4 inactivation peptide (RCK4-IP) shows a similar spatial distribution of charged and uncharged regions, but is more flexible and less ordered in its amino-terminal part.
About this StructureAbout this Structure
1ZTO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
NMR structure of inactivation gates from mammalian voltage-dependent potassium channels., Antz C, Geyer M, Fakler B, Schott MK, Guy HR, Frank R, Ruppersberg JP, Kalbitzer HR, Nature. 1997 Jan 16;385(6613):272-5. PMID:9000078
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