1ztn
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INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, 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
1ZTN 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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