1bgk
From Proteopedia
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| - | [[Image:1bgk.gif|left|200px]]<br /><applet load="1bgk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1bgk" /> | ||
| - | '''SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES'''<br /> | ||
| - | == | + | ==SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES== |
| + | <StructureSection load='1bgk' size='340' side='right'caption='[[1bgk]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1bgk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bunodosoma_granuliferum Bunodosoma granuliferum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BGK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 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=1bgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgk OCA], [https://pdbe.org/1bgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bgk RCSB], [https://www.ebi.ac.uk/pdbsum/1bgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/K1B_BUNGR K1B_BUNGR] Inhibits voltage-dependent potassium channels of the Kv1 family (Kv1.1/KCNA1 (Kd=6 nM), Kv1.2/KCNA2 (Kd=15 nM), Kv1.3/KCNA3 (Kd=10-39 nM), Kv1.6/KCNA6, and KCa3.1/KCNN4 (Kd=172 nM)).<ref>PMID:10419508</ref> <ref>PMID:10585444</ref> <ref>PMID:11707459</ref> <ref>PMID:8098956</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
BgK is a K+ channel-blocking toxin from the sea anemone Bunodosoma granulifera. It is a 37-residue protein that adopts a novel fold, as determined by NMR and modeling. An alanine-scanning-based analysis revealed the functional importance of five residues, which include a critical lysine and an aromatic residue separated by 6.6 +/- 1.0 A. The same diad is found in the three known homologous toxins from sea anemones. More strikingly, a similar functional diad is present in all K+ channel-blocking toxins from scorpions, although these toxins adopt a distinct scaffold. Moreover, the functional diads of potassium channel-blocking toxins from sea anemone and scorpions superimpose in the three-dimensional structures. Therefore, toxins that have unrelated structures but similar functions possess conserved key functional residues, organized in an identical topology, suggesting a convergent functional evolution for these small proteins. | BgK is a K+ channel-blocking toxin from the sea anemone Bunodosoma granulifera. It is a 37-residue protein that adopts a novel fold, as determined by NMR and modeling. An alanine-scanning-based analysis revealed the functional importance of five residues, which include a critical lysine and an aromatic residue separated by 6.6 +/- 1.0 A. The same diad is found in the three known homologous toxins from sea anemones. More strikingly, a similar functional diad is present in all K+ channel-blocking toxins from scorpions, although these toxins adopt a distinct scaffold. Moreover, the functional diads of potassium channel-blocking toxins from sea anemone and scorpions superimpose in the three-dimensional structures. Therefore, toxins that have unrelated structures but similar functions possess conserved key functional residues, organized in an identical topology, suggesting a convergent functional evolution for these small proteins. | ||
| - | + | On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures.,Dauplais M, Lecoq A, Song J, Cotton J, Jamin N, Gilquin B, Roumestand C, Vita C, de Medeiros CL, Rowan EG, Harvey AL, Menez A J Biol Chem. 1997 Feb 14;272(7):4302-9. PMID:9020148<ref>PMID:9020148</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1bgk" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bunodosoma granuliferum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cotton J]] | ||
| + | [[Category: Dauplais M]] | ||
| + | [[Category: Gilquin B]] | ||
| + | [[Category: Harvey A]] | ||
| + | [[Category: Jamin N]] | ||
| + | [[Category: Lecoq A]] | ||
| + | [[Category: Menez A]] | ||
| + | [[Category: Roumestand C]] | ||
| + | [[Category: Song J]] | ||
| + | [[Category: Vita C]] | ||
Current revision
SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES
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Categories: Bunodosoma granuliferum | Large Structures | Cotton J | Dauplais M | Gilquin B | Harvey A | Jamin N | Lecoq A | Menez A | Roumestand C | Song J | Vita C
