Molecular moulds with multiple missions: functional sites in three-finger toxins.
1. Snake venoms are complex mixtures of pharmacologically active peptides and proteins. 2. These protein toxins belong to a small number of superfamilies of proteins. The present review describes structure-function relationships of three-finger toxins. 3. All toxins share a common structure of three beta-stranded loops extending from a central core. However, they bind to different receptors/acceptors and exhibit a wide variety of biological effects. 4. Thus, the structure-function relationships of this group of toxins are complicated and challenging. 5. Studies have shown that the functional sites in these "sibling" toxins are located on various segments of the molecular surface.
Kini
R Manjunatha
RM
Department of Biological Sciences, Faculty of Science, National University of Singapore, 10 Kent Ridge Crescent, Singapore 119260. dbskinim@nus.edu.sg
D000818:Animals; D001208:Asia; D001315:Australia; D006801:Humans; D008958:Models, Molecular; D009498:Neurotoxins / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D012910:Snake Venoms / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D013329:Structure-Activity Relationship
D009498:Neurotoxins; D012910:Snake Venoms