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1sco

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(New page: 200px<br /><applet load="1sco" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sco" /> '''SCORPION TOXIN (OSK1 TOXIN) WITH HIGH AFFINI...)
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[[Image:1sco.gif|left|200px]]<br /><applet load="1sco" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sco" />
 
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'''SCORPION TOXIN (OSK1 TOXIN) WITH HIGH AFFINITY FOR SMALL CONDUCTANCE CA(2+)-ACTIVATED K+ CHANNEL IN NEUROBLASTOMA-X-GLUOMA NG 108-15 HYBRID CELLS, NMR, 30 STRUCTURES'''<br />
 
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==Overview==
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==SCORPION TOXIN (OSK1 TOXIN) WITH HIGH AFFINITY FOR SMALL CONDUCTANCE CA(2+)-ACTIVATED K+ CHANNEL IN NEUROBLASTOMA-X-GLUOMA NG 108-15 HYBRID CELLS, NMR, 30 STRUCTURES==
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A 600 MHz 1H NMR study of toxin OSK1, blocker of small-conductance, Ca2+-activated K+ channels, is presented. The unambiguous sequential, assignment of all the protons of the toxin was obtained using TOCSY, DQF-COSY, and NOESY experiments at pH 3.0 (10, 30, and 45 degrees C) in, aqueous solution. 3J(N alpha), 3J(alphabeta) vicinal spin coupling, constants were determined in high-resolution spectra. The cross-peak, volumes in NOESY spectra and the coupling constants were used to define, the local structure of the protein by the program HABAS and to generate, torsion angle and interproton distance constraints for the program DIANA., Hydrogen-deuterium exchange rates of amide protons showed possible, locations of hydrogen bonds. The hydrogen bond acceptors and disulfide, bridges between residues 8-28, 14-33, and 18-35 were determined when, analyzing distance distribution in preliminary DIANA structures. All, constraints were used to obtain a set of 30 structures by DIANA. The, resulting rms deviations over 30 structures are 1.30 A for the heavy atoms, and 0.42 A for the backbone heavy atoms. The structures were refined by, constrained energy minimization using the SYBYL program. Their analysis, indicated the existence of the alpha-helix (residues 10-21) slightly, distorted at the Cys14 residue, two main strands of the antiparallel, beta-sheet (24-29, 32-38), and the extended fragment (2-6). The motif is, stabilized by the disulfide bridges in the way, common to all known, scorpion toxins. Using the fine spatial toxin structure, alignment of the, homologues, mutagenesis analysis, and comparison of scorpion toxin family, functions, we delineate some differences significant for the toxin, specificity.
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<StructureSection load='1sco' size='340' side='right'caption='[[1sco]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1sco]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Orthochirus_scrobiculosus Orthochirus scrobiculosus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sco OCA], [https://pdbe.org/1sco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sco RCSB], [https://www.ebi.ac.uk/pdbsum/1sco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sco ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KAX37_ORTSC KAX37_ORTSC] Blocks voltage-gated potassium channels Kv1.1/KCNA1 (IC(50)=0.6nM), Kv1.2/KCNA2 (IC(50)=5.4nM), Kv1.3/KCNA3 (IC(50)=0.014nM) potently, and moderately block intermediate conductance calcium-activated potassium channels KCa3.1/KCNN4 (IC(50)=225nM). At high concentration (2 mM), is also active on Kv1.6/KCNA6 and Shaker IR.[REFERENCE:1]<ref>PMID:15588251</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sc/1sco_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sco ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1SCO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Orthochirus_scrobiculosus Orthochirus scrobiculosus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SCO OCA].
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*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
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== References ==
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==Reference==
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<references/>
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Three-dimensional structure of toxin OSK1 from Orthochirus scrobiculosus scorpion venom., Jaravine VA, Nolde DE, Reibarkh MJ, Korolkova YV, Kozlov SA, Pluzhnikov KA, Grishin EV, Arseniev AS, Biochemistry. 1997 Feb 11;36(6):1223-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9063870 9063870]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Orthochirus scrobiculosus]]
[[Category: Orthochirus scrobiculosus]]
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[[Category: Single protein]]
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[[Category: Arseniev AS]]
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[[Category: Arseniev, A.S.]]
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[[Category: Grishin EV]]
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[[Category: Grishin, E.V.]]
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[[Category: Jaravine VA]]
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[[Category: Jaravine, V.A.]]
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[[Category: Nolde DE]]
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[[Category: Nolde, D.E.]]
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[[Category: Pluzhnikov KA]]
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[[Category: Pluzhnikov, K.A.]]
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[[Category: potassium channel inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:16:44 2007''
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Current revision

SCORPION TOXIN (OSK1 TOXIN) WITH HIGH AFFINITY FOR SMALL CONDUCTANCE CA(2+)-ACTIVATED K+ CHANNEL IN NEUROBLASTOMA-X-GLUOMA NG 108-15 HYBRID CELLS, NMR, 30 STRUCTURES

PDB ID 1sco

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