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1ztn
From Proteopedia
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[[Image:1ztn.gif|left|200px]] | [[Image:1ztn.gif|left|200px]] | ||
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'''INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES''' | '''INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES''' | ||
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[[Category: Ruppersberg, J P.]] | [[Category: Ruppersberg, J P.]] | ||
[[Category: Schott, M.]] | [[Category: Schott, M.]] | ||
| - | [[Category: | + | [[Category: Inactivation gate]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | [[Category: | + | [[Category: Potassium channel]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:03:33 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:03, 3 May 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 Sat May 3 18:03:33 2008
