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1ztn
From Proteopedia
(New page: 200px<br /><applet load="1ztn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ztn" /> '''INACTIVATION GATE OF POTASSIUM CHANNEL RAW3,...) |
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| - | [[Image:1ztn.gif|left|200px]]<br /><applet load="1ztn" size=" | + | [[Image:1ztn.gif|left|200px]]<br /><applet load="1ztn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ztn" /> | caption="1ztn" /> | ||
'''INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES'''<br /> | '''INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, 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== | ||
| - | 1ZTN 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:// | + | 1ZTN 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=1ZTN 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 16:18:57 2008'' |
Revision as of 14:18, 21 February 2008
|
INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES
Overview
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
1ZTN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 16:18:57 2008
