1mah
From Proteopedia
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| - | [[Image:1mah.gif|left|200px]] | + | [[Image:1mah.gif|left|200px]] |
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| - | '''FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX''' | + | {{Structure |
| + | |PDB= 1mah |SIZE=350|CAPTION= <scene name='initialview01'>1mah</scene>, resolution 3.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= MOUSE ACHE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MAH is a [ | + | 1MAH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAH OCA]. |
==Reference== | ==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:[http:// | + | Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex., Bourne Y, Taylor P, Marchot P, Cell. 1995 Nov 3;83(3):503-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8521480 8521480] |
[[Category: Acetylcholinesterase]] | [[Category: Acetylcholinesterase]] | ||
[[Category: Dendroaspis angusticeps]] | [[Category: Dendroaspis angusticeps]] | ||
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[[Category: venom]] | [[Category: venom]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:00 2008'' |
Revision as of 10:41, 20 March 2008
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| , resolution 3.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | MOUSE ACHE (Mus musculus) | ||||||
| Activity: | Acetylcholinesterase, with EC number 3.1.1.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 12:41:00 2008
