1m2s

From Proteopedia

(Difference between revisions)

Revision as of 18:49, 29 November 2023

Solution Structure of A New Potassium Channels Blocker from the Venom of Chinese Scorpion Buthus martensi Karsch

Structural highlights

1m2s is a 1 chain structure with sequence from Mesobuthus martensii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KA162_MESMA Alpha-KTx 16.2: inhibits large conductance calcium-activated potassium channels (KCa1.1/Slo-beta4 KCNMA1/KCNMB4). It appears to block channel activity by a simple bimolecular inhibition process. Shows a fast association rate and a slow dissociation rate of binding on rat brain synaptosome (PubMed:18199674). Significantly inhibits voltage-dependent sodium current and voltage-dependent delayed rectifier potassium currents (PubMed:14632928).^[1] ^[2] Martentoxin-1: significantly inhibits voltage-dependent sodium current (Nav) and voltage-dependent delayed rectifier potassium current.^[3]

Publication Abstract from PubMed

This article reports the solution structure of BmTx3B (alpha-KTx16.2), a potassium channel blocker belonging to the subfamily alpha-KTx16, purified from the venom of the Chinese scorpion Buthus martensi Karsch. In solution, BmTx3B assumes a typical CSalphabeta motif, with an alpha-helix connected to a triple-stranded beta-sheet by 3 disulfide bridges, which belongs to the first structural group of short-chain scorpion toxins. On the other hand, BmTx3B is quite different from other toxins (such as ChTx and AgTx2) of this group in terms of the electrostatic and hydrophobic surface distribution. The functional surface (beta-face) of the molecule is characterized by less basic residues (only 2: Lys28 and Arg35) and extra aromatic residues (Phe1, Phe9, Trp15, and Tyr37). The peptide shows a great preference for the Kca1.1 channel over the Kv channel (about a 10(3)-fold difference). The model of BmTx3B/Kca1.1 channel complex generated by docking and dynamic simulation reveals that the stable binding between the BmTx3B and Kca1.1 channel is favored by a number of aromatic pi-pi stacking interactions. The influences of these structural features on the kinetic behavior of the toxin binding to Kca1.1 channel are also discussed.

The solution structure of BmTx3B, a member of the scorpion toxin subfamily alpha-KTx 16.,Wang Y, Chen X, Zhang N, Wu G, Wu H Proteins. 2005 Feb 1;58(2):489-97. PMID:15558557^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cao ZY, Shen WQ, Pan YP, Xiao X, Liu XM, Wang XL, Liang XT, Yu DQ. Purification, characterization of two peptides from Buthus martensi Karch. J Pept Res. 2003 Dec;62(6):252-9. PMID:14632928
↑ Shi J, He HQ, Zhao R, Duan YH, Chen J, Chen Y, Yang J, Zhang JW, Shu XQ, Zheng P, Ji YH. Inhibition of martentoxin on neuronal BK channel subtype (alpha+beta4): implications for a novel interaction model. Biophys J. 2008 May 1;94(9):3706-13. doi: 10.1529/biophysj.107.122150. Epub 2008 , Jan 16. PMID:18199674 doi:http://dx.doi.org/10.1529/biophysj.107.122150
↑ Cao ZY, Shen WQ, Pan YP, Xiao X, Liu XM, Wang XL, Liang XT, Yu DQ. Purification, characterization of two peptides from Buthus martensi Karch. J Pept Res. 2003 Dec;62(6):252-9. PMID:14632928
↑ Wang Y, Chen X, Zhang N, Wu G, Wu H. The solution structure of BmTx3B, a member of the scorpion toxin subfamily alpha-KTx 16. Proteins. 2005 Feb 1;58(2):489-97. PMID:15558557 doi:10.1002/prot.20322

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m2s"

Categories: Large Structures | Mesobuthus martensii | Hu G | Li M | Wang Y | Wu G | Wu H | Zhang N

@@ Line 1: / Line 1: @@
 ==Solution Structure of A New Potassium Channels Blocker from the Venom of Chinese Scorpion Buthus martensi Karsch==
-<StructureSection load='1m2s' size='340' side='right'caption='[[1m2s]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+<StructureSection load='1m2s' size='340' side='right'caption='[[1m2s]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1m2s]] 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=1M2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M2S FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1big|1big]], [[2bmt|2bmt]], [[2crd|2crd]], [[1lir|1lir]]</div></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'>[https://proteopedia.org/fgij/fg.htm?mol=1m2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2s OCA], [https://pdbe.org/1m2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m2s RCSB], [https://www.ebi.ac.uk/pdbsum/1m2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m2s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KA162_MESMA KA162_MESMA]] Alpha-KTx 16.2: inhibits large conductance calcium-activated potassium channels (KCa1.1/Slo-beta4 KCNMA1/KCNMB4). It appears to block channel activity by a simple bimolecular inhibition process. Shows a fast association rate and a slow dissociation rate of binding on rat brain synaptosome (PubMed:18199674). Significantly inhibits voltage-dependent sodium current and voltage-dependent delayed rectifier potassium currents (PubMed:14632928).<ref>PMID:14632928</ref> <ref>PMID:18199674</ref>   Martentoxin-1: significantly inhibits voltage-dependent sodium current (Nav) and voltage-dependent delayed rectifier potassium current.<ref>PMID:14632928</ref>
+[https://www.uniprot.org/uniprot/KA162_MESMA KA162_MESMA] Alpha-KTx 16.2: inhibits large conductance calcium-activated potassium channels (KCa1.1/Slo-beta4 KCNMA1/KCNMB4). It appears to block channel activity by a simple bimolecular inhibition process. Shows a fast association rate and a slow dissociation rate of binding on rat brain synaptosome (PubMed:18199674). Significantly inhibits voltage-dependent sodium current and voltage-dependent delayed rectifier potassium currents (PubMed:14632928).<ref>PMID:14632928</ref> <ref>PMID:18199674</ref>   Martentoxin-1: significantly inhibits voltage-dependent sodium current (Nav) and voltage-dependent delayed rectifier potassium current.<ref>PMID:14632928</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 27: @@
 [[Category: Large Structures]]
 [[Category: Mesobuthus martensii]]
-[[Category: Hu, G]]
+[[Category: Hu G]]
-[[Category: Li, M]]
+[[Category: Li M]]
-[[Category: Wang, Y]]
+[[Category: Wang Y]]
-[[Category: Wu, G]]
+[[Category: Wu G]]
-[[Category: Wu, H]]
+[[Category: Wu H]]
-[[Category: Zhang, N]]
+[[Category: Zhang N]]
-[[Category: Alpha/beta scaffold]]
-[[Category: Toxin]]

1m2s

From Proteopedia

Revision as of 18:49, 29 November 2023

Solution Structure of A New Potassium Channels Blocker from the Venom of Chinese Scorpion Buthus martensi Karsch

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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