3dd4: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
<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=3dd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dd4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3dd4 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=3dd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dd4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3dd4 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/KCIP4_MOUSE KCIP4_MOUSE]] Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Probably modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND3/Kv4.3 and KCND2/Kv4.2 currents (By similarity).<ref>PMID:11805342</ref> <ref>PMID:19109250</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 20:09, 24 December 2014
Structural Basis of KChIP4a Modulation of Kv4.3 Slow InactivationStructural Basis of KChIP4a Modulation of Kv4.3 Slow Inactivation
Structural highlights
Function[KCIP4_MOUSE] Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Probably modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND3/Kv4.3 and KCND2/Kv4.2 currents (By similarity).[1] [2] Publication Abstract from PubMedDynamic inactivation in Kv4 A-type K(+) current plays a critical role in regulating neuronal excitability by shaping action potential waveform and duration. Multifunctional auxiliary KChIP1-4 subunits, which share a high homology in their C-terminal core regions, exhibit distinctive modulation of inactivation and surface expression of pore-forming Kv4 subunits. However, the structural differences that underlie the functional diversity of Kv channel-interacting proteins (KChIPs) remain undetermined. Here we have described the crystal structure of KChIP4a at 3.0A resolution, which shows distinct N-terminal alpha-helices that differentiate it from other KChIPs. Biochemical experiments showed that competitive binding of the Kv4.3 N-terminal peptide to the hydrophobic groove of the core of KChIP4a causes the release of the KChIP4a N terminus that suppresses the inactivation of Kv4.3 channels. Electrophysiology experiments confirmed that the first N-terminal alpha-helix peptide (residues 1-34) of KChIP4a, either by itself or fused to N-terminal truncated Kv4.3, can confer slow inactivation. We propose that N-terminal binding of Kv4.3 to the core of KChIP4a mobilizes the KChIP4a N terminus, which serves as the slow inactivation gate. Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation.,Liang P, Wang H, Chen H, Cui Y, Gu L, Chai J, Wang K J Biol Chem. 2009 Feb 20;284(8):4960-7. Epub 2008 Dec 24. PMID:19109250[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||