1zto: Difference between revisions

Revision as of 21:38, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zto.png

Template:STRUCTURE 1zto

INACTIVATION GATE OF POTASSIUM CHANNEL RCK4, NMR, 8 STRUCTURESINACTIVATION GATE OF POTASSIUM CHANNEL RCK4, NMR, 8 STRUCTURES

Template:ABSTRACT PUBMED 9000078

About this StructureAbout this Structure

1ZTO is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

NMR structure of inactivation gates from mammalian voltage-dependent potassium channels., Antz C, Geyer M, Fakler B, Schott MK, Guy HR, Frank R, Ruppersberg JP, Kalbitzer HR, Nature. 1997 Jan 16;385(6613):272-5. PMID:9000078

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1zto|  PDB=1zto  |  SCENE=  }}
-'''INACTIVATION GATE OF POTASSIUM CHANNEL RCK4, NMR, 8 STRUCTURES'''
+===INACTIVATION GATE OF POTASSIUM CHANNEL RCK4, NMR, 8 STRUCTURES===
-==Overview==
+<!--
-The electrical signalling properties of neurons originate largely from the gating properties of their ion channels. N-type inactivation of voltage-gated potassium (Kv) channels is the best-understood gating transition in ion channels, and occurs by a 'ball-and-chain' type mechanism. In this mechanism an N-terminal domain (inactivation gate), which is tethered to the cytoplasmic side of the channel protein by a protease-cleavable chain, binds to its receptor at the inner vestibule of the channel, thereby physically blocking the pore. Even when synthesized as a peptide, ball domains restore inactivation in Kv channels whose inactivation domains have been deleted. Using high-resolution nuclear magnetic resonance (NMR) spectroscopy, we analysed the three-dimensional structure of the ball peptides from two rapidly inactivating mammalian K. channels (Raw3 (Kv3.4) and RCK4 (Kv1.4)). The inactivation peptide of Raw3 (Raw3-IP) has a compact structure that exposes two phosphorylation sites and allows the formation of an intramolecular disulphide bridge between two spatially close cysteine residues. Raw3-IP exhibits a characteristic surface charge pattern with a positively charged, a hydrophobic, and a negatively charged region. The RCK4 inactivation peptide (RCK4-IP) shows a similar spatial distribution of charged and uncharged regions, but is more flexible and less ordered in its amino-terminal part.
+The line below this paragraph, {{ABSTRACT_PUBMED_9000078}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9000078 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9000078}}
 ==About this Structure==
-ZTO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZTO OCA].
+ZTO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZTO OCA].
 ==Reference==
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 [[Category: Nmr]]
 [[Category: Potassium channel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:03:35 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:38:28 2008''