X-ray Crystallographic Studies on Acetylcholinesterase and Related Enzymes
Abstract
The principal objectives of this contract are to better understand the mechanism of action of AChE, and to characterize its various ligand-binding sites. These objectives are being approached by the method of single crystal X-ray diffraction, together with time-resolved X-ray crystallography, using Torpedo californica AChE (TcAChE) as the principal source of enzyme. Computational molecular model building and electrostatic characterization are being used as complementary theoretical approaches. Attempts are also being made to crystallize, and if successful, to solve the 3D structures of cholinesterases (ChEs) from other sources. These include human recombinant AChE, bovine fetal serum AChE, AChE from the venom of the krait, Bungarus fasciatus (BfAChE), and horse serum BChE. Homology model building will be used to compare and analyze the structures of these enzymes. In parallel, we are attempting to express and crystallize, with the eventual objective of solving its 3D structure, human serum paraoxonase/arylesterase.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 1999
- Accession Number
- ADA365388
Entities
People
- I. Silman
- J. L. Sussman
Organizations
- Weizmann Institute of Science