1b4g
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(New page: 200px<br /> <applet load="1b4g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b4g" /> '''CONTROL OF K+ CHANNEL GATING BY PROTEIN PHO...)
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Revision as of 13:59, 12 November 2007
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CONTROL OF K+ CHANNEL GATING BY PROTEIN PHOSPHORYLATION: STRUCTURAL SWITCHES OF THE INACTIVATION GATE, NMR, 22 STRUCTURES
Overview
Fast N-type inactivation of voltage-dependent potassium (Kv) channels, controls membrane excitability and signal propagation in central neurons, and occurs by a 'ball-and-chain'-type mechanism. In this mechanism an, N-terminal protein domain (inactivation gate) occludes the pore from the, cytoplasmic side. In Kv3.4 channels, inactivation is not fixed but is, dynamically regulated by protein phosphorylation. Phosphorylation of, several identified serine residues on the inactivation gate leads to, reduction or removal of fast inactivation. Here, we investigate the, structure-function basis of this phospho-regulation with nuclear magnetic, resonance (NMR) spectroscopy and patch-clamp recordings using synthetic, inactivation domains (ID). The dephosphorylated ID exhibited compact, structure and displayed high-affinity binding to its receptor., Phosphorylation of serine residues in the N- or C-terminal half of the ID, resulted in a loss of overall structural stability. However, depending on, the residue(s) phosphorylated, distinct structural elements remained, stable. These structural changes correlate with the distinct changes in, binding and unbinding kinetics underlying the reduced inactivation potency, of phosphorylated IDs.
About this Structure
1B4G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Control of K+ channel gating by protein phosphorylation: structural switches of the inactivation gate., Antz C, Bauer T, Kalbacher H, Frank R, Covarrubias M, Kalbitzer HR, Ruppersberg JP, Baukrowitz T, Fakler B, Nat Struct Biol. 1999 Feb;6(2):146-50. PMID:10048926
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