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1bgk

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(New page: 200px<br /><applet load="1bgk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bgk" /> '''SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY F...)
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[[Image:1bgk.gif|left|200px]]<br /><applet load="1bgk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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'''SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES'''<br />
 
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==Overview==
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==SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES==
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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.
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<StructureSection load='1bgk' size='340' side='right'caption='[[1bgk]]' scene=''>
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== Structural highlights ==
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<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>
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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=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>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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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1BGK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bunodosoma_granulifera Bunodosoma granulifera]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BGK 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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9020148 9020148]
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</div>
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[[Category: Bunodosoma granulifera]]
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<div class="pdbe-citations 1bgk" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Cotton, J.]]
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[[Category: Dauplais, M.]]
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[[Category: Gilquin, B.]]
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[[Category: Harvey, A.]]
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[[Category: Jamin, N.]]
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[[Category: Lecoq, A.]]
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[[Category: Menez, A.]]
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[[Category: Roumestand, C.]]
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[[Category: Song, J.]]
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[[Category: Vita, C.]]
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[[Category: neurotoxin]]
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[[Category: potassium channel inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:38:19 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: Bunodosoma granuliferum]]
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[[Category: Large Structures]]
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[[Category: Cotton J]]
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[[Category: Dauplais M]]
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[[Category: Gilquin B]]
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[[Category: Harvey A]]
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[[Category: Jamin N]]
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[[Category: Lecoq A]]
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[[Category: Menez A]]
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[[Category: Roumestand C]]
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[[Category: Song J]]
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[[Category: Vita C]]

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SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES

PDB ID 1bgk

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