1ztn: Difference between revisions

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 ==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=''>
+<StructureSection load='1ztn' size='340' side='right'caption='[[1ztn]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ztn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
+<table><tr><td colspan='2'>[[1ztn]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1ZTN FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KCNC4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ztn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ztn OCA], [http://pdbe.org/1ztn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ztn RCSB], [http://www.ebi.ac.uk/pdbsum/1ztn PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ztn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ztn OCA], [https://pdbe.org/1ztn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ztn RCSB], [https://www.ebi.ac.uk/pdbsum/1ztn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ztn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KCNC4_HUMAN KCNC4_HUMAN]] This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
+[https://www.uniprot.org/uniprot/KCNC4_HUMAN KCNC4_HUMAN] This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
-<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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ztn" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Potassium Channel|Potassium Channel]]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Antz, C]]
+[[Category: Large Structures]]
-[[Category: Fakler, B]]
+[[Category: Antz C]]
-[[Category: Frank, R]]
+[[Category: Fakler B]]
-[[Category: Geyer, M]]
+[[Category: Frank R]]
-[[Category: Guy, H R]]
+[[Category: Geyer M]]
-[[Category: Kalbitzer, H R]]
+[[Category: Guy HR]]
-[[Category: Ruppersberg, J P]]
+[[Category: Kalbitzer HR]]
-[[Category: Schott, M]]
+[[Category: Ruppersberg JP]]
-[[Category: Inactivation gate]]
+[[Category: Schott M]]
-[[Category: Potassium channel]]
-[[Category: Transport protein]]