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1ztn

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[[Image:1ztn.gif|left|200px]]
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{{Seed}}
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[[Image:1ztn.png|left|200px]]
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{{STRUCTURE_1ztn| PDB=1ztn | SCENE= }}
{{STRUCTURE_1ztn| PDB=1ztn | SCENE= }}
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'''INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES'''
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===INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_9000078}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9000078 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9000078}}
==About this Structure==
==About this Structure==
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1ZTN is a [[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].
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1ZTN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZTN OCA].
==Reference==
==Reference==
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[[Category: Nmr]]
[[Category: Nmr]]
[[Category: Potassium channel]]
[[Category: Potassium channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:03:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:54:01 2008''

Revision as of 11:54, 27 July 2008

Image:1ztn.png

Template:STRUCTURE 1ztn

INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES

Template:ABSTRACT PUBMED 9000078

About this Structure

1ZTN is a Single protein structure of sequence from Homo sapiens. Full experimental 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

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