5foq
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Acetylcholinesterase in complex with C7653== | |
| + | <StructureSection load='5foq' size='340' side='right' caption='[[5foq]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5foq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FOQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GC8:2-(2,4-DICHLOROPHENOXY)-N-[4-(1-PIPERIDINYLMETHYL)PHENYL]ACETAMIDE'>GC8</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=P15:2,5,8,11,14,17-HEXAOXANONADECAN-19-OL'>P15</scene>, <scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fpp|5fpp]], [[5fpq|5fpq]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5foq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5foq OCA], [http://pdbe.org/5foq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5foq RCSB], [http://www.ebi.ac.uk/pdbsum/5foq PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Molecular recognition events in biological systems are driven by non-covalent interactions between interacting species. Here, we have studied hydrogen bonds of the CHY type involving electron-deficient CH donors using dispersion-corrected density functional theory (DFT) calculations applied to acetylcholinesterase-ligand complexes. The strengths of CHY interactions activated by a proximal cation were considerably strong; comparable to or greater than those of classical hydrogen bonds. Significant differences in the energetic components compared to classical hydrogen bonds and non-activated CHY interactions were observed. Comparison between DFT and molecular mechanics calculations showed that common force fields could not reproduce the interaction energy values of the studied hydrogen bonds. The presented results highlight the importance of considering CHY interactions when analysing protein-ligand complexes, call for a review of current force fields, and opens up possibilities for the development of improved design tools for drug discovery. | ||
| - | + | The Nature of Activated Non-classical Hydrogen Bonds: A Case Study on Acetylcholinesterase-Ligand Complexes.,Berg L, Mishra BK, Andersson CD, Ekstrom F, Linusson A Chemistry. 2016 Feb;22(8):2672-81. doi: 10.1002/chem.201503973. Epub 2016 Jan 11. PMID:26751405<ref>PMID:26751405</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5foq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acetylcholinesterase]] | ||
| + | [[Category: Andersson, D C]] | ||
| + | [[Category: Berg, L]] | ||
[[Category: Ekstrom, F]] | [[Category: Ekstrom, F]] | ||
| - | [[Category: Mishra, B.K]] | ||
[[Category: Linusson, A]] | [[Category: Linusson, A]] | ||
| - | [[Category: | + | [[Category: Mishra, B K]] |
| - | [[Category: | + | [[Category: Density functional theory]] |
| + | [[Category: Drug design]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Quantum chemistry]] | ||
| + | [[Category: Signaling protein]] | ||
Revision as of 15:03, 2 March 2016
Acetylcholinesterase in complex with C7653
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