1b4g: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1b4g.gif|left|200px]]
{{Seed}}
[[Image:1b4g.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1b4g|  PDB=1b4g  |  SCENE=  }}  
{{STRUCTURE_1b4g|  PDB=1b4g  |  SCENE=  }}  


'''CONTROL OF K+ CHANNEL GATING BY PROTEIN PHOSPHORYLATION: STRUCTURAL SWITCHES OF THE INACTIVATION GATE, NMR, 22 STRUCTURES'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_10048926}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10048926 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10048926}}


==About this Structure==
==About this Structure==
1B4G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4G OCA].  
1B4G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4G OCA].  


==Reference==
==Reference==
Line 34: Line 38:
[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
[[Category: Potassium channel]]
[[Category: Potassium channel]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:03:21 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:13:58 2008''

Revision as of 15:14, 30 June 2008

File:1b4g.png

Template:STRUCTURE 1b4g

CONTROL OF K+ CHANNEL GATING BY PROTEIN PHOSPHORYLATION: STRUCTURAL SWITCHES OF THE INACTIVATION GATE, NMR, 22 STRUCTURES

Template:ABSTRACT PUBMED 10048926

About this Structure

1B4G is a Single protein structure of sequence from Escherichia coli. Full experimental 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

Page seeded by OCA on Mon Jun 30 18:13:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1b4g&oldid=575925"