Picture map of Europe with pins indicating European capital cities

Open Access research with a European policy impact...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by Strathclyde researchers, including by researchers from the European Policies Research Centre (EPRC).

EPRC is a leading institute in Europe for comparative research on public policy, with a particular focus on regional development policies. Spanning 30 European countries, EPRC research programmes have a strong emphasis on applied research and knowledge exchange, including the provision of policy advice to EU institutions and national and sub-national government authorities throughout Europe.

Explore research outputs by the European Policies Research Centre...

On the convergent evolution of animal toxins - conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures

Dauplais, M. and Lecoq, A. and Song, J.X. and Cotton, J. and Jamin, N. and Gilquin, B. and Rowan, E.G. and Vita, C. (1997) On the convergent evolution of animal toxins - conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. Journal of Biological Chemistry, 272 (7). pp. 4302-4309. ISSN 1083-351X

Full text not available in this repository. Request a copy from the Strathclyde author

Abstract

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 Å. 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.