1mah: Difference between revisions

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[[Image:1mah.gif|left|200px]]
{{Seed}}
[[Image:1mah.png|left|200px]]


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{{STRUCTURE_1mah|  PDB=1mah  |  SCENE=  }}  
{{STRUCTURE_1mah|  PDB=1mah  |  SCENE=  }}  


'''FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX'''
===FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_8521480}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_8521480}}


==About this Structure==
==About this Structure==
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[[Category: Toxin]]
[[Category: Toxin]]
[[Category: Venom]]
[[Category: Venom]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:49:35 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:33:36 2008''

Revision as of 20:33, 2 July 2008

File:1mah.png

Template:STRUCTURE 1mah

FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX

Template:ABSTRACT PUBMED 8521480

About this Structure

1MAH is a Protein complex structure of sequences from Dendroaspis angusticeps and Mus musculus. Full crystallographic information is available from OCA.

Reference

Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex., Bourne Y, Taylor P, Marchot P, Cell. 1995 Nov 3;83(3):503-12. PMID:8521480

Page seeded by OCA on Wed Jul 2 23:33:36 2008

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