1mah
From Proteopedia
(New page: 200px<br /><applet load="1mah" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mah, resolution 3.2Å" /> '''FASCICULIN2-MOUSE ACE...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mah.gif|left|200px]]<br /><applet load="1mah" size=" | + | [[Image:1mah.gif|left|200px]]<br /><applet load="1mah" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mah, resolution 3.2Å" /> | caption="1mah, resolution 3.2Å" /> | ||
'''FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX'''<br /> | '''FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the snake toxin fasciculin, bound to mouse | + | 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== | ==About this Structure== | ||
| - | 1MAH is a [http://en.wikipedia.org/wiki/Protein_complex 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] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1MAH is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAH OCA]. |
==Reference== | ==Reference== | ||
| Line 25: | Line 25: | ||
[[Category: venom]] | [[Category: venom]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:13 2008'' |
Revision as of 11:53, 21 February 2008
|
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 with as ligand. Active as Acetylcholinesterase, with EC number 3.1.1.7 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 Feb 21 13:53:13 2008
