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==Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch== | |||
<StructureSection load='1q2k' size='340' side='right'caption='[[1q2k]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1q2k]] 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=1Q2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q2K FirstGlance]. <br> | |||
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 21 models</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=1q2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q2k OCA], [https://pdbe.org/1q2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q2k RCSB], [https://www.ebi.ac.uk/pdbsum/1q2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q2k ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KA191_MESMA KA191_MESMA] Selective inhibitor of high conductance calcium-activated potassium channels KCa1.1/KCNMA1. May be insect specific.<ref>PMID:15178692</ref> [PDB:3E8Y] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
BmBKTx1 is a 31-amino acid peptide identified from the venom of the Chinese scorpion Buthus martensi Karsch, blocking high-conductance calcium-activated potassium channels. Sequence homology analysis indicates that BmBKTx1 is a new subfamily of short-chain alpha-KTx toxins of the potassium channel, which we term alpha-KTx19. Synthetic BmBKTx1 was prepared by using solid-phase peptide synthesis. Two-dimensional NMR spectroscopy techniques were used to determine the solution structure of BmBKTx1. The results show that the BmBKTx1 forms a typical cysteine-stabilized alpha/beta scaffold adopted by most short-chain scorpion toxins. The structure of BmBKTx1 consists of a two-stranded antiparallel beta-sheet (residues 20-29) and an alpha-helix (residues 5-15). The three-dimensional structure of BmBKTx1 was also compared with those of two function-related scorpion toxins, charybdotoxin (ChTx) and BmTx1, and their structural and functional implications are discussed. | BmBKTx1 is a 31-amino acid peptide identified from the venom of the Chinese scorpion Buthus martensi Karsch, blocking high-conductance calcium-activated potassium channels. Sequence homology analysis indicates that BmBKTx1 is a new subfamily of short-chain alpha-KTx toxins of the potassium channel, which we term alpha-KTx19. Synthetic BmBKTx1 was prepared by using solid-phase peptide synthesis. Two-dimensional NMR spectroscopy techniques were used to determine the solution structure of BmBKTx1. The results show that the BmBKTx1 forms a typical cysteine-stabilized alpha/beta scaffold adopted by most short-chain scorpion toxins. The structure of BmBKTx1 consists of a two-stranded antiparallel beta-sheet (residues 20-29) and an alpha-helix (residues 5-15). The three-dimensional structure of BmBKTx1 was also compared with those of two function-related scorpion toxins, charybdotoxin (ChTx) and BmTx1, and their structural and functional implications are discussed. | ||
Solution structure of BmBKTx1, a new BKCa1 channel blocker from the Chinese scorpion Buthus martensi Karsch.,Cai Z, Xu C, Xu Y, Lu W, Chi CW, Shi Y, Wu J Biochemistry. 2004 Apr 6;43(13):3764-71. PMID:15049683<ref>PMID:15049683</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1q2k" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mesobuthus martensii]] | |||
[[Category: Cai Z]] | |||
[[Category: Chi CW]] | |||
[[Category: Lu W]] | |||
[[Category: Shi Y]] | |||
[[Category: Wu J]] | |||
[[Category: Xu C]] | |||
[[Category: Xu Y]] | |||
Latest revision as of 10:24, 9 October 2024
Solution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi KarschSolution structure of BmBKTx1 a new potassium channel blocker from the Chinese Scorpion Buthus martensi Karsch
Structural highlights
FunctionKA191_MESMA Selective inhibitor of high conductance calcium-activated potassium channels KCa1.1/KCNMA1. May be insect specific.[1] [PDB:3E8Y] Publication Abstract from PubMedBmBKTx1 is a 31-amino acid peptide identified from the venom of the Chinese scorpion Buthus martensi Karsch, blocking high-conductance calcium-activated potassium channels. Sequence homology analysis indicates that BmBKTx1 is a new subfamily of short-chain alpha-KTx toxins of the potassium channel, which we term alpha-KTx19. Synthetic BmBKTx1 was prepared by using solid-phase peptide synthesis. Two-dimensional NMR spectroscopy techniques were used to determine the solution structure of BmBKTx1. The results show that the BmBKTx1 forms a typical cysteine-stabilized alpha/beta scaffold adopted by most short-chain scorpion toxins. The structure of BmBKTx1 consists of a two-stranded antiparallel beta-sheet (residues 20-29) and an alpha-helix (residues 5-15). The three-dimensional structure of BmBKTx1 was also compared with those of two function-related scorpion toxins, charybdotoxin (ChTx) and BmTx1, and their structural and functional implications are discussed. Solution structure of BmBKTx1, a new BKCa1 channel blocker from the Chinese scorpion Buthus martensi Karsch.,Cai Z, Xu C, Xu Y, Lu W, Chi CW, Shi Y, Wu J Biochemistry. 2004 Apr 6;43(13):3764-71. PMID:15049683[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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