Abstract：
:The crystal structure of the snake toxin fasciculin, bound to mouse acetylcholinesterase (mAChE), at 3.2 A resolution reveals a synergistic three-point anchorage consistent with the picomolar dissociation constant of the complex. Loop II of fasciculin contains a cluster of hydrophobic residues that interact with the peripheral anionic site of the enzyme and sterically occlude substrate access to the catalytic site. Loop I fits in a crevice near the lip of the gorge to maximize the surface area of contact of loop II at the gorge entry. The fasciculin core surrounds a protruding loop on the enzyme surface and stabilizes the whole assembly. Upon binding of fasciculin, subtle structural rearrangements of AChE occur that could explain the observed residual catalytic activity of the fasciculin-enzyme complex.
journal_name
Celljournal_title
Cellauthors
Bourne Y,Taylor P,Marchot Pdoi
10.1016/0092-8674(95)90128-0subject
Has Abstractpub_date
1995-11-03 00:00:00pages
503-12issue
3eissn
0092-8674issn
1097-4172pii
0092-8674(95)90128-0journal_volume
83pub_type
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