1pvz

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(New page: 200px<br /><applet load="1pvz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pvz" /> '''Solution Structure of BmP07, A Novel Potassi...)
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[[Image:1pvz.gif|left|200px]]<br /><applet load="1pvz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pvz" />
 
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'''Solution Structure of BmP07, A Novel Potassium Channel Blocker from Scorpion Buthus martensi Karsch, 15 structures'''<br />
 
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==Overview==
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==Solution Structure of BmP07, A Novel Potassium Channel Blocker from Scorpion Buthus martensi Karsch, 15 structures==
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A natural K+ channel blocker, BmKK2 (a member of scorpion toxin subfamily, alpha-KTx 14), which is composed of 31 amino acid residues and purified, from the venom of the Chinese scorpion Buthus martensi Karsch, was, characterized using whole-cell patch-clamp recording in rat hippocampal, neurons. The three dimensional structure of BmKK2 was determined with, two-dimensional NMR spectroscopy and molecular modelling techniques. In, solution this toxin adopted a common alpha/beta-motif, but showed distinct, local conformation in the loop between alpha-helix and beta-sheet in, comparison with typical short-chain scorpion toxins (e.g., CTX and NTX)., Also, the alpha helix is shorter and the beta-sheet element is smaller, (each strand consisted only two residues). The unusual structural feature, of BmKK2 was attributed to the shorter loop between the alpha-helix and, beta-sheet and the presence of two consecutive Pro residues at position 21, and 22 in the loop. Moreover, two models of BmKK2/hKv1.3 channel and, BmKK2/rSK2 channel complexes were simulated with docking calculations. The, results demonstrated the existence of a alpha-mode binding between the, toxin and the channels. The model of BmKK2/rSK2 channel complex exhibited, favorable contacts both in electrostatic and hydrophobic, including a, network of five hydrogen bonds and bigger interface containing seven pairs, of inter-residue interactions. In contrast, the model of BmKK2/hKv1.3, channel complex, containing only three pairs of inter-residue, interactions, exhibited poor contacts and smaller interface. The results, well explained its lower activity towards Kv channel, and predicted that, it may prefer a type of SK channel with a narrower entryway as its, specific receptor.
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<StructureSection load='1pvz' size='340' side='right'caption='[[1pvz]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1pvz]] 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=1PVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PVZ 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=1pvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pvz OCA], [https://pdbe.org/1pvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pvz RCSB], [https://www.ebi.ac.uk/pdbsum/1pvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pvz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KA142_MESMA KA142_MESMA] Inhibits potassium channels. May be active towards small conductance calcium-activated potassium channels (KCNN, SK), and less active towards voltage-gated potassium channels (Kv/KCN).<ref>PMID:15146482</ref> <ref>PMID:15208022</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A natural K+ channel blocker, BmKK2 (a member of scorpion toxin subfamily alpha-KTx 14), which is composed of 31 amino acid residues and purified from the venom of the Chinese scorpion Buthus martensi Karsch, was characterized using whole-cell patch-clamp recording in rat hippocampal neurons. The three dimensional structure of BmKK2 was determined with two-dimensional NMR spectroscopy and molecular modelling techniques. In solution this toxin adopted a common alpha/beta-motif, but showed distinct local conformation in the loop between alpha-helix and beta-sheet in comparison with typical short-chain scorpion toxins (e.g., CTX and NTX). Also, the alpha helix is shorter and the beta-sheet element is smaller (each strand consisted only two residues). The unusual structural feature of BmKK2 was attributed to the shorter loop between the alpha-helix and beta-sheet and the presence of two consecutive Pro residues at position 21 and 22 in the loop. Moreover, two models of BmKK2/hKv1.3 channel and BmKK2/rSK2 channel complexes were simulated with docking calculations. The results demonstrated the existence of a alpha-mode binding between the toxin and the channels. The model of BmKK2/rSK2 channel complex exhibited favorable contacts both in electrostatic and hydrophobic, including a network of five hydrogen bonds and bigger interface containing seven pairs of inter-residue interactions. In contrast, the model of BmKK2/hKv1.3 channel complex, containing only three pairs of inter-residue interactions, exhibited poor contacts and smaller interface. The results well explained its lower activity towards Kv channel, and predicted that it may prefer a type of SK channel with a narrower entryway as its specific receptor.
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==About this Structure==
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Solution structure of BmKK2, a new potassium channel blocker from the venom of chinese scorpion Buthus martensi Karsch.,Zhang N, Li M, Chen X, Wang Y, Wu G, Hu G, Wu H Proteins. 2004 Jun 1;55(4):835-45. PMID:15146482<ref>PMID:15146482</ref>
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1PVZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PVZ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Solution structure of BmKK2, a new potassium channel blocker from the venom of chinese scorpion Buthus martensi Karsch., Zhang N, Li M, Chen X, Wang Y, Wu G, Hu G, Wu H, Proteins. 2004 Jun 1;55(4):835-45. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15146482 15146482]
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</div>
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[[Category: Mesobuthus martensii]]
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<div class="pdbe-citations 1pvz" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Hu, G.]]
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[[Category: Li, M.]]
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[[Category: Ou, L.]]
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[[Category: Wang, Y.]]
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[[Category: Wu, H.]]
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[[Category: Zhang, N.]]
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[[Category: Zhang, Q.]]
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[[Category: alpha/beta scaffold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:10:23 2007''
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==See Also==
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*[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mesobuthus martensii]]
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[[Category: Hu G]]
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[[Category: Li M]]
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[[Category: Ou L]]
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[[Category: Wang Y]]
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[[Category: Wu H]]
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[[Category: Zhang N]]
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[[Category: Zhang Q]]

Current revision

Solution Structure of BmP07, A Novel Potassium Channel Blocker from Scorpion Buthus martensi Karsch, 15 structures

PDB ID 1pvz

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