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1b4i

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Revision as of 06:04, 17 August 2017

Control of K+ Channel Gating by protein phosphorylation: structural switches of the inactivation gate, NMR, 22 structures

Structural highlights

1b4i is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KCNC4_HUMAN] This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Antz C, Bauer T, Kalbacher H, Frank R, Covarrubias M, Kalbitzer HR, Ruppersberg JP, Baukrowitz T, Fakler B. Control of K+ channel gating by protein phosphorylation: structural switches of the inactivation gate. Nat Struct Biol. 1999 Feb;6(2):146-50. PMID:10048926 doi:10.1038/5833

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b4i"

@@ Line 1: / Line 1: @@
 ==Control of K+ Channel Gating by protein phosphorylation: structural switches of the inactivation gate, NMR, 22 structures==
 <StructureSection load='1b4i' size='340' side='right' caption='[[1b4i]], [[NMR_Ensembles_of_Models | 23 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1b4i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B4I FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1b4i]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B4I FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4i OCA], [http://pdbe.org/1b4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b4i RCSB], [http://www.ebi.ac.uk/pdbsum/1b4i PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4i OCA], [http://pdbe.org/1b4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b4i RCSB], [http://www.ebi.ac.uk/pdbsum/1b4i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b4i ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
 [[Category: Antz, C]]
 [[Category: Bauer, T]]

1b4i

From Proteopedia

Revision as of 06:04, 17 August 2017

Control of K+ Channel Gating by protein phosphorylation: structural switches of the inactivation gate, NMR, 22 structures

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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