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1mah

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[[Image:1mah.gif|left|200px]]
 
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{{Structure
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==FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX==
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|PDB= 1mah |SIZE=350|CAPTION= <scene name='initialview01'>1mah</scene>, resolution 3.2&Aring;
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<StructureSection load='1mah' size='340' side='right'caption='[[1mah]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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<table><tr><td colspan='2'>[[1mah]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MAH FirstGlance]. <br>
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|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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mah OCA], [https://pdbe.org/1mah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mah RCSB], [https://www.ebi.ac.uk/pdbsum/1mah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mah ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACES_MOUSE ACES_MOUSE] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ma/1mah_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mah ConSurf].
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<div style="clear:both"></div>
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'''FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX'''
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==See Also==
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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*[[Fasciculin|Fasciculin]]
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==Overview==
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__TOC__
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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.
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</StructureSection>
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Acetylcholinesterase]]
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[[Category: Dendroaspis angusticeps]]
[[Category: Dendroaspis angusticeps]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Bourne Y]]
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[[Category: Bourne, Y.]]
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[[Category: Marchot P]]
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[[Category: Marchot, P.]]
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[[Category: Taylor P]]
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[[Category: Taylor, P.]]
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[[Category: NAG]]
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[[Category: hydrolase]]
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[[Category: serine esterase]]
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[[Category: synapse]]
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[[Category: toxin]]
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[[Category: venom]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:00 2008''
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Current revision

FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX

PDB ID 1mah

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