Structural highlights
Function
ACES_MOUSE Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
Publication Abstract from PubMed
Take a closer look: Unexpectedly, a pair of enantiomeric ligands proved to have similar binding affinities for acetylcholinesterase. Further studies indicated that the enantiomers exhibit different thermodynamic profiles. Analyses of the noncovalent interactions in the protein-ligand complexes revealed that these differences are partly due to nonclassical hydrogen bonds between the ligands and aromatic side chains of the protein.
Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase.,Berg L, Niemiec MS, Qian W, Andersson CD, Wittung-Stafshede P, Ekstrom F, Linusson A Angew Chem Int Ed Engl. 2012 Nov 19. doi: 10.1002/anie.201205113. PMID:23161758[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Berg L, Niemiec MS, Qian W, Andersson CD, Wittung-Stafshede P, Ekstrom F, Linusson A. Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase. Angew Chem Int Ed Engl. 2012 Nov 19. doi: 10.1002/anie.201205113. PMID:23161758 doi:http://dx.doi.org/10.1002/anie.201205113
