1bgk: Difference between revisions
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'''SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES''' | {{Structure | ||
|PDB= 1bgk |SIZE=350|CAPTION= <scene name='initialview01'>1bgk</scene> | |||
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'''SEA ANEMONE TOXIN (BGK) WITH HIGH AFFINITY FOR VOLTAGE DEPENDENT POTASSIUM CHANNEL, NMR, 15 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BGK is a [ | 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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9020148 9020148] | ||
[[Category: Bunodosoma granulifera]] | [[Category: Bunodosoma granulifera]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: potassium channel inhibitor]] | [[Category: potassium channel inhibitor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:42 2008'' | ||
Revision as of 08:10, 20 March 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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