1bgk

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

Structural highlights

1bgk is a 1 chain structure with sequence from Bunodosoma granuliferum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 15 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

K1B_BUNGR Inhibits voltage-dependent potassium channels of the Kv1 family (Kv1.1/KCNA1 (Kd=6 nM), Kv1.2/KCNA2 (Kd=15 nM), Kv1.3/KCNA3 (Kd=10-39 nM), Kv1.6/KCNA6, and KCa3.1/KCNN4 (Kd=172 nM)).[1] [2] [3] [4]

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[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Rauer H, Pennington M, Cahalan M, Chandy KG. Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin. J Biol Chem. 1999 Jul 30;274(31):21885-92. PMID:10419508 doi:10.1074/jbc.274.31.21885
  2. ↑ Alessandri-Haber N, Lecoq A, Gasparini S, Grangier-Macmath G, Jacquet G, Harvey AL, de Medeiros C, Rowan EG, Gola M, Ménez A, Crest M. Mapping the functional anatomy of BgK on Kv1.1, Kv1.2, and Kv1.3. Clues to design analogs with enhanced selectivity. J Biol Chem. 1999 Dec 10;274(50):35653-61. PMID:10585444 doi:10.1074/jbc.274.50.35653
  3. ↑ Racapé J, Lecoq A, Romi-Lebrun R, Liu J, Kohler M, Garcia ML, Ménez A, Gasparini S. Characterization of a novel radiolabeled peptide selective for a subpopulation of voltage-gated potassium channels in mammalian brain. J Biol Chem. 2002 Feb 8;277(6):3886-93. PMID:11707459 doi:10.1074/jbc.M109886200
  4. ↑ Aneiros A, García I, Martínez JR, Harvey AL, Anderson AJ, Marshall DL, Engström A, Hellman U, Karlsson E. A potassium channel toxin from the secretion of the sea anemone Bunodosoma granulifera. Isolation, amino acid sequence and biological activity. Biochim Biophys Acta. 1993 May 7;1157(1):86-92. PMID:8098956 doi:10.1016/0304-4165(93)90082-j
  5. ↑ 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. On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J Biol Chem. 1997 Feb 14;272(7):4302-9. PMID:9020148
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