ALTERNATIVE ENTRANCES OPENING IN ACETYLCHOLINESTERASE
| Authors | |
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| Year of publication | 2009 |
| Type | Conference abstract |
| MU Faculty or unit | |
| Citation | |
| Description | Alternative entrances and their involvement in the catalytic cycle of acetylcholinesterase as potential routes of product clearance is a long discussed subject in the field of acetylcholinesterase chemistry. The phenomenon of alternative entrances was discovered by computational chemistry methods and there are several supporting and also disproving experimental evidences. In our study, we focussed on further investigation of this issue and found new dynamical structural features of acetylcholinesterase active site together with different alternative entrances opening frequency as compared to results previously reported. The main difference lies in a flap-like motion of Trp86 residue in the mouse acetylcholinesterase (pdb code 1N5M) and the opening frequency is much larger. We attribute these findings to a different force field and starting acetylcholinesterase structure used. |
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