1bgk

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{{STRUCTURE_1bgk| PDB=1bgk | SCENE= }}
{{STRUCTURE_1bgk| PDB=1bgk | SCENE= }}
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'''SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES'''
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===SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES===
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==Overview==
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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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{{ABSTRACT_PUBMED_9020148}}
==About this Structure==
==About this Structure==
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1BGK is a [[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].
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1BGK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bunodosoma_granulifera Bunodosoma granulifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGK OCA].
==Reference==
==Reference==
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[[Category: Neurotoxin]]
[[Category: Neurotoxin]]
[[Category: Potassium channel inhibitor]]
[[Category: Potassium channel inhibitor]]
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Revision as of 16:06, 30 June 2008

Template:STRUCTURE 1bgk

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

Template:ABSTRACT PUBMED 9020148

About this Structure

1BGK is a Single protein structure of sequence from Bunodosoma granulifera. Full experimental 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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