6td2: Difference between revisions
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Mus musculus Acetylcholinesterase in complex with N-(2-(diethylamino)ethyl)-1-(4-(trifluoromethyl)phenyl)methanesulfonamide== | ==Mus musculus Acetylcholinesterase in complex with N-(2-(diethylamino)ethyl)-1-(4-(trifluoromethyl)phenyl)methanesulfonamide== | ||
<StructureSection load='6td2' size='340' side='right'caption='[[6td2]]' scene=''> | <StructureSection load='6td2' size='340' side='right'caption='[[6td2]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TD2 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TD2 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ETE:2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>ETE</scene>, <scene name='pdbligand=N2K:~{N}-[2-(diethylamino)ethyl]-1-[4-(trifluoromethyl)phenyl]methanesulfonamide'>N2K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6td2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6td2 OCA], [https://pdbe.org/6td2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6td2 RCSB], [https://www.ebi.ac.uk/pdbsum/6td2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6td2 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Arene-arene interactions play important roles in protein-ligand complex formation. Here, we investigate the characteristics of arene-arene interactions between small organic molecules and aromatic amino acids in protein interiors. The study is based on X-ray crystallographic data and quantum mechanical calculations using the enzyme acetylcholinesterase and selected inhibitory ligands as a model system. It is shown that the arene substituents of the inhibitors dictate the strength of the interaction and the geometry of the resulting complexes. Importantly, the calculated interaction energies correlate well with the measured inhibitor potency. Non-hydrogen substituents strengthened all interaction types in the protein milieu, in keeping with results for benzene dimer model systems. The interaction energies were dispersion-dominated, but substituents that induced local dipole moments increased the electrostatic contribution and thus yielded more strongly bound complexes. These findings provide fundamental insights into the physical mechanisms governing arene-arene interactions in the protein milieu and thus into molecular recognition between proteins and small molecules. | |||
Physical Mechanisms Governing Substituent Effects on Arene-Arene Interactions in a Protein Milieu.,Andersson CD, Mishra BK, Forsgren N, Ekstrom F, Linusson A J Phys Chem B. 2020 Jul 30;124(30):6529-6539. doi: 10.1021/acs.jpcb.0c03778. Epub, 2020 Jul 20. PMID:32610016<ref>PMID:32610016</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6td2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 13:30, 23 October 2024
Mus musculus Acetylcholinesterase in complex with N-(2-(diethylamino)ethyl)-1-(4-(trifluoromethyl)phenyl)methanesulfonamideMus musculus Acetylcholinesterase in complex with N-(2-(diethylamino)ethyl)-1-(4-(trifluoromethyl)phenyl)methanesulfonamide
Structural highlights
Publication Abstract from PubMedArene-arene interactions play important roles in protein-ligand complex formation. Here, we investigate the characteristics of arene-arene interactions between small organic molecules and aromatic amino acids in protein interiors. The study is based on X-ray crystallographic data and quantum mechanical calculations using the enzyme acetylcholinesterase and selected inhibitory ligands as a model system. It is shown that the arene substituents of the inhibitors dictate the strength of the interaction and the geometry of the resulting complexes. Importantly, the calculated interaction energies correlate well with the measured inhibitor potency. Non-hydrogen substituents strengthened all interaction types in the protein milieu, in keeping with results for benzene dimer model systems. The interaction energies were dispersion-dominated, but substituents that induced local dipole moments increased the electrostatic contribution and thus yielded more strongly bound complexes. These findings provide fundamental insights into the physical mechanisms governing arene-arene interactions in the protein milieu and thus into molecular recognition between proteins and small molecules. Physical Mechanisms Governing Substituent Effects on Arene-Arene Interactions in a Protein Milieu.,Andersson CD, Mishra BK, Forsgren N, Ekstrom F, Linusson A J Phys Chem B. 2020 Jul 30;124(30):6529-6539. doi: 10.1021/acs.jpcb.0c03778. Epub, 2020 Jul 20. PMID:32610016[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||