1wm7: Difference between revisions
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==Solution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch, 9 structures== | ==Solution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch, 9 structures== | ||
<StructureSection load='1wm7' size='340' side='right' caption='[[1wm7 | <StructureSection load='1wm7' size='340' side='right'caption='[[1wm7]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1wm7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1wm7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WM7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wm7 OCA], [https://pdbe.org/1wm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wm7 RCSB], [https://www.ebi.ac.uk/pdbsum/1wm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wm7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KAX82_MESMA KAX82_MESMA] Blocks small conductance calcium-activated potassium channels (KCNN, SK). Low toxicity by intracerebroventricular injection into mice.<ref>PMID:22511981</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Potassium channel toxin|Potassium channel toxin]] | *[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mesobuthus martensii]] | [[Category: Mesobuthus martensii]] | ||
[[Category: Chen | [[Category: Chen X]] | ||
[[Category: He | [[Category: He F]] | ||
[[Category: Hu | [[Category: Hu G]] | ||
[[Category: Jiang | [[Category: Jiang S]] | ||
[[Category: Li | [[Category: Li Y]] | ||
[[Category: Wei | [[Category: Wei D]] | ||
[[Category: Wu | [[Category: Wu G]] | ||
[[Category: Wu | [[Category: Wu H]] | ||
Latest revision as of 12:28, 6 December 2023
Solution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch, 9 structuresSolution Structure of BmP01 from the Venom of Scorpion Buthus martensii Karsch, 9 structures
Structural highlights
FunctionKAX82_MESMA Blocks small conductance calcium-activated potassium channels (KCNN, SK). Low toxicity by intracerebroventricular injection into mice.[1] Publication Abstract from PubMedFrom the venom of scorpion Buthus martensii Karsch,a short peptide (BmP01, 29 amino acid residues) was isolated and characterized as previously reported (Lebren, R. R., et al. (1997) Eur. J. Biochem. 245, 457-464). It was shown to reduce 33% outward K(+) channel (hippocampal neurons) currents at 10 microM. The solution structure of BmP01 was determined by 2D (1)H NMR spectroscopy. The NOEs, coupling constants, and H-D exchange obtained from NMR spectroscopy were used in structural calculations. The conformation of BmP01 is composed of a short alpha-helix (Cys 3-Thr 12) and a two-stranded antiparallel beta-sheet (Ala 15-Asp 20 and Lys 23-Pro 28). There are three disulfide bridges (Cys 3-Cys 19, Cys 6-Cys 24 and Cys 10-Cys 26) connecting the alpha-helix and beta-sheet. Asp 20 to Lys 23 form a type II turn linking the two strands. Structural and electrostatic potential comparison between BmP01 and its analogues are also presented. Solution structure of BmP01 from the venom of scorpion Buthus martensii Karsch.,Wu G, Li Y, Wei D, He F, Jiang S, Hu G, Wu H Biochem Biophys Res Commun. 2000 Oct 5;276(3):1148-54. PMID:11027603[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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