|Influence of ligand binding on the conformation of Torpedo californica acetylcholinesterase|Boutonnet, N.; Van Belle, D.; Wodak, S.J. (2001). Influence of ligand binding on the conformation of Torpedo californica acetylcholinesterase. Theoretical Chemistry Accounts 106(1-2): 10-21. dx.doi.org/10.1007/s002140000226
In: Theoretical Chemistry Accounts. Springer: New York. ISSN 1432-881X, more
structural changes; acetylcholinesterase; structure alignment program
|Authors|| || Top |
- Boutonnet, N.
- Van Belle, D.
- Wodak, S.J.
With the aim of identifying structural changes in acetylcholinesterase, induced by ligand binding, we use a completely automatic procedure to analyse the differences between the backbone conformation of the free enzyme and those in eight complexes of Torpedo californica acetylcholinesterase, with various quaternary ammonium ligands, and with the protein inhibitor fasciculin. In order to discriminate between structural changes due to ligand binding and those arising from model imprecision, we also examine protein–ligand and protein–water contacts. Except for the peptide flip in the complex with huperzine A, the backbones of other complexes with quaternary ammonium ligands display negligible changes relative to the free enzyme. Another exception is the complex with the bisquaternary ammonium ligand decamethonium, where several loops display above average deformations, but only two, those spanning residues 334–348 and residues 277–304, seem to move as a result of ligand binding. Movement of the ω loop (residues 61–95) is detected only in the complex with the protein fasciculin.