Structural comparison of three crystalline complexes of a peptidic toxin with a synaptic acetylcholine recognition protein.
Many peptidic toxins from animal venoms target neuronal or peripheral synaptic receptors with high affinities and specificities. Hence, these toxins are not only potent natural weapons but also precise molecular tools for pharmacological studies of their receptors. Although they belong to various structural and/or functional subfamilies, they often share similar molecular features, such as a highly reticulated scaffold presenting specific binding determinants.
Bourne
Yves
Y
Architecture et Fonction des Macromolécules Biologiques, CNRS, Marseille, France.
Hansen
Scott B
SB
Sulzenbacher
Gerlind
G
Talley
Todd T
TT
Huxford
Tom
T
Taylor
Palmer
P
Marchot
Pascale
P
D000109:Acetylcholine / Q000378:metabolism*; D000818:Animals; D002800:Cholinesterase Inhibitors; D004546:Elapid Venoms / Q000737:chemistry*; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D013569:Synapses / Q000502:physiology*
D002800:Cholinesterase Inhibitors; D004546:Elapid Venoms; D009419:Nerve Tissue Proteins; D010455:Peptides; C044937:fasciculin; D000109:Acetylcholine