1bgk
From Proteopedia
(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=" | + | [[Image:1bgk.gif|left|200px]]<br /><applet load="1bgk" size="350" 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 /> | '''SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BgK is a K+ channel-blocking toxin from the sea anemone Bunodosoma | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: potassium channel inhibitor]] | [[Category: potassium channel inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:02 2008'' |
Revision as of 09:55, 21 February 2008
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SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES
Overview
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.
About this Structure
1BGK is a Single protein structure of sequence from Bunodosoma granulifera. Full crystallographic information is available from OCA.
Reference
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
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