2xud: Difference between revisions

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-{{Seed}}
-[[Image:2xud.jpg|left|200px]]
-<!--
+==Crystal structure of the Y337A mutant of mouse acetylcholinesterase==
-The line below this paragraph, containing "STRUCTURE_2xud", creates the "Structure Box" on the page.
+<StructureSection load='2xud' size='340' side='right'caption='[[2xud]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2xud]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XUD FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DME:DECAMETHONIUM+ION'>DME</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>
-{{STRUCTURE_2xud|  PDB=2xud  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xud OCA], [https://pdbe.org/2xud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xud RCSB], [https://www.ebi.ac.uk/pdbsum/2xud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xud ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The active center of acetylcholinesterase (AChE), a target site for competitive inhibitors, resides centrosymmetric to the subunit at the base of a deep, narrow gorge lined by aromatic residues. At the gorge entry, a peripheral site encompasses overlapping binding loci for noncompetitive inhibitors, which alter substrate access to the gorge. The click-chemistry inhibitor TZ2PA6 links the active center ligand, tacrine, to the peripheral site ligand, propidium, through a biorthogonal reaction of an acetylene and an azide that forms either a syn1 or an anti1 triazole. Compared with wild-type mouse AChE, a Tyr337Ala mutant displays full catalytic activity, albeit with 2-3 orders of magnitude higher affinities for the TZ2PA6 syn1 and anti1 regioisomers, reflected in low femtomolar K(d) values, diffusion-limited association, and dissociation half-times greater than 1 month and 1 week, respectively. Three structures of each of the co-crystallized syn1 and anti1 complexes of the Tyr337Ala mutant were solved at three distinct times of crystal maturation, consistent with or exceeding the half-lives of the complexes in solution, while crystalline complexes obtained from soaked Tyr337Ala crystals led to picturing "freshly formed" complexes. The structures, at 2.55-2.75A resolution, reveal a range of unprecedented conformations of the bound regioisomers, not observed in the wild-type AChE complexes, associated with concerted positional rearrangements of side chains in the enzyme gorge. Moreover, time-dependent conformational remodeling of the crystalline complexes appears to correlate with the dissociation half-times of the solution complexes. Hence, for the tight-binding TZ2PA6 inhibitors, the initial complexes kinetically driven in solution slowly form more stable complexes governed by thermodynamic equilibrium and observable in mature crystals.
-===CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE ACETYLCHOLINESTERASE===
+Conformational Remodeling of Femtomolar Inhibitor-Acetylcholinesterase Complexes in the Crystalline State.,Bourne Y, Radic Z, Taylor P, Marchot P J Am Chem Soc. 2010 Nov 19. PMID:21090615<ref>PMID:21090615</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2xud" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_21090615}}, adds the Publication Abstract to the page
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 21090615 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21090615}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-XUD is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XUD OCA].
-==Reference==
-<ref group="xtra">PMID:21090615</ref><references group="xtra"/>
-[[Category: Acetylcholinesterase]]
 [[Category: Mus musculus]]
-[[Category: Bourne, Y.]]
+[[Category: Bourne Y]]
-[[Category: Marchot, P.]]
+[[Category: Marchot P]]
-[[Category: Radic, Z.]]
+[[Category: Radic Z]]
-[[Category: Taylor, P.]]
+[[Category: Taylor P]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec  8 11:46:21 2010''