Comparison of sea anemone and scorpion toxins binding to Kv1 channels: an example of convergent evolution.
Comparison of data from functional mapping carried out on scorpion and sea anemones toxins blocking currents through voltage-gated potassium channels revealed that, despite their different 3D structures, the binding cores of these toxins displayed some similarities. Further molecular modeling studies suggested that these similarities reflect the use by these toxins of a common binding mode to exert their blocking function. Therefore, scorpion and sea anemone toxins offer an example of mechanistic convergent evolution.
Gasparini
Sylvaine
S
Département d'Ingénierie et d'Etudes des Protéines, CEA Saclay, 91191 Gif sur Yvette cedex, France.
Gilquin
Bernard
B
Ménez
André
A
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003064:Cnidarian Venoms / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015221:Potassium Channels / Q000378:metabolism*; D011485:Protein Binding; D012604:Scorpion Venoms / Q000737:chemistry / Q000378:metabolism*; D012605:Scorpions / Q000737:chemistry*; D012615:Sea Anemones / Q000737:chemistry*; D016415:Sequence Alignment; D013329:Structure-Activity Relationship
D003064:Cnidarian Venoms; D015221:Potassium Channels; D012604:Scorpion Venoms