1mah

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[[Image:1mah.gif|left|200px]]
[[Image:1mah.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1mah |SIZE=350|CAPTION= <scene name='initialview01'>1mah</scene>, resolution 3.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1mah", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= MOUSE ACHE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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-->
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|DOMAIN=
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{{STRUCTURE_1mah| PDB=1mah | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mah OCA], [http://www.ebi.ac.uk/pdbsum/1mah PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mah RCSB]</span>
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}}
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'''FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX'''
'''FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX'''
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[[Category: Marchot, P.]]
[[Category: Marchot, P.]]
[[Category: Taylor, P.]]
[[Category: Taylor, P.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: serine esterase]]
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[[Category: Serine esterase]]
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[[Category: synapse]]
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[[Category: Synapse]]
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[[Category: toxin]]
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[[Category: Toxin]]
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[[Category: venom]]
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[[Category: Venom]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:49:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:32 2008''
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Revision as of 21:49, 2 May 2008

Image:1mah.gif

Template:STRUCTURE 1mah

FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX


Overview

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.

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 Sat May 3 00:49:35 2008

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