This is an old revision of this page, as edited by ProteinBoxBot(talk | contribs) at 06:00, 20 May 2016(Updating to new gene infobox populated via wikidata). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.
Revision as of 06:00, 20 May 2016 by ProteinBoxBot(talk | contribs)(Updating to new gene infobox populated via wikidata)
KCNA4 (Kv1.4) contains a tandem inactivation domain at the N terminus. It is composed of two subdomains. Inactivation domain 1 (ID1, residues 1-38) consists of a flexible N terminus anchored at a 5-turn helix, and is thought to work by occluding the ion pathway, as is the case with a classical ball domain. Inactivation domain 2 (ID2, residues 40-50) is a 2.5 turn helix with a high proportion of hydrophobic residues that probably serves to attach ID1 to the cytoplasmic face of the channel. In this way, it can promote rapid access of ID1 to the receptor site in the open channel. ID1 and ID2 function together to bring about fast inactivation of the Kv1.4 channel, which is important for the role of the channel in short-term plasticity.[9]
^Oudit GY, Kassiri Z, Sah R, Ramirez RJ, Zobel C, Backx PH (May 2001). "The molecular physiology of the cardiac transient outward potassium current (I(to)) in normal and diseased myocardium". J. Mol. Cell. Cardiol. 33 (5): 851–72. doi:10.1006/jmcc.2001.1376. PMID11343410.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^Wissmann R, Bildl W, Oliver D, Beyermann M, Kalbitzer HR, Bentrop D, Fakler B (May 2003). "Solution structure and function of the "tandem inactivation domain" of the neuronal A-type potassium channel Kv1.4". J. Biol. Chem. 278 (18): 16142–50. doi:10.1074/jbc.M210191200. PMID12590144.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
^ abInanobe, Atsushi; Fujita Akikazu; Ito Minoru; Tomoike Hitonobu; Inageda Kiyoshi; Kurachi Yoshihisa (Jun 2002). "Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic membrane of excitatory synapses". Am. J. Physiol., Cell Physiol. 282 (6). United States: C1396–403. doi:10.1152/ajpcell.00615.2001. ISSN0363-6143. PMID11997254. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)
^Niethammer, M; Valtschanoff J G; Kapoor T M; Allison D W; Weinberg R J; Craig A M; Sheng M (Apr 1998). "CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90". Neuron. 20 (4). UNITED STATES: 693–707. doi:10.1016/S0896-6273(00)81009-0. ISSN0896-6273. PMID9581762. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)
^ abKim, E; Sheng M (1996). "Differential K+ channel clustering activity of PSD-95 and SAP97, two related membrane-associated putative guanylate kinases". Neuropharmacology. 35 (7). ENGLAND: 993–1000. doi:10.1016/0028-3908(96)00093-7. ISSN0028-3908. PMID8938729. {{cite journal}}: Cite has empty unknown parameters: |laysummary=, |laydate=, and |laysource= (help)
^Eldstrom, Jodene; Doerksen Kyle W; Steele David F; Fedida David (Nov 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Lett. 531 (3). Netherlands: 529–37. doi:10.1016/S0014-5793(02)03572-X. ISSN0014-5793. PMID12435606. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)
^Coleman, S K; Newcombe J; Pryke J; Dolly J O (Aug 1999). "Subunit composition of Kv1 channels in human CNS". J. Neurochem. 73 (2). UNITED STATES: 849–58. doi:10.1046/j.1471-4159.1999.0730849.x. ISSN0022-3042. PMID10428084. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)
^Eldstrom, Jodene; Choi Woo Sung; Steele David F; Fedida David (Jul 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Lett. 547 (1–3). Netherlands: 205–11. doi:10.1016/S0014-5793(03)00668-9. ISSN0014-5793. PMID12860415. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)
