View source for 1bgk


==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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bgk" style="background-color:#fffaf0;"></div>

==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]]