1ztn: Difference between revisions

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-[[Image:1ztn.png|left|200px]]
+==INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES==
+<StructureSection load='1ztn' size='340' side='right' caption='[[1ztn]], [[NMR_Ensembles_of_Models | 8 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ztn]] is a 1 chain structure with 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=1ZTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZTN FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ztn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ztn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ztn RCSB], [http://www.ebi.ac.uk/pdbsum/1ztn PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-{{STRUCTURE_1ztn|  PDB=1ztn  |  SCENE=  }}
+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<ref>PMID:9000078</ref>
-===INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_9000078}}
-==About this Structure==
-[[1ztn]] is a 1 chain structure with 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=1ZTN OCA].
 ==See Also==
 *[[Potassium Channel|Potassium Channel]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:009000078</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
 [[Category: Antz, C.]]