Ontology highlight
ABSTRACT:
SUBMITTER: Xu Y
PROVIDER: S-EPMC2517048 | biostudies-literature | 2008 Sep
REPOSITORIES: biostudies-literature
Xu Yechun Y Colletier Jacques-Philippe JP Weik Martin M Jiang Hualiang H Moult John J Silman Israel I Sussman Joel L JL
Biophysical journal 20080523 5
The high aromatic content of the deep and narrow active-site gorge of acetylcholinesterase (AChE) is a remarkable feature of this enzyme. Here, we analyze conformational flexibility of the side chains of the 14 conserved aromatic residues in the active-site gorge of Torpedo californica AChE based on the 47 three-dimensional crystal structures available for the native enzyme, and for its complexes and conjugates, and on a 20-ns molecular dynamics (MD) trajectory of the native enzyme. The degree o ...[more]