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1bgk
From Proteopedia
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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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Revision as of 09:31, 20 November 2007
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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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