1bgk: Difference between revisions
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==SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES== | |||
<StructureSection load='1bgk' size='340' side='right' caption='[[1bgk]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1bgk]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BGK FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bgk RCSB], [http://www.ebi.ac.uk/pdbsum/1bgk PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Potassium channel toxin|Potassium channel toxin]] | *[[Potassium channel toxin|Potassium channel toxin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Bunodosoma granuliferum]] | [[Category: Bunodosoma granuliferum]] | ||
[[Category: Cotton, J | [[Category: Cotton, J]] | ||
[[Category: Dauplais, M | [[Category: Dauplais, M]] | ||
[[Category: Gilquin, B | [[Category: Gilquin, B]] | ||
[[Category: Harvey, A | [[Category: Harvey, A]] | ||
[[Category: Jamin, N | [[Category: Jamin, N]] | ||
[[Category: Lecoq, A | [[Category: Lecoq, A]] | ||
[[Category: Menez, A | [[Category: Menez, A]] | ||
[[Category: Roumestand, C | [[Category: Roumestand, C]] | ||
[[Category: Song, J | [[Category: Song, J]] | ||
[[Category: Vita, C | [[Category: Vita, C]] | ||
[[Category: Neurotoxin]] | [[Category: Neurotoxin]] | ||
[[Category: Potassium channel inhibitor]] | [[Category: Potassium channel inhibitor]] | ||
