Cholinesterase structure: Identification of residues and domains affecting organophosphate inhibition and catalysis. Annual report, 6 March 1995-5 March 1996
Technical Report
·
OSTI ID:381617
In the initial year of the grant, we have made excellent progress in several arenas: (1) A crystal structure of a mouse acetylcholinesterase-fasciculin 2 complex has been solved. (2) Studies with enantiomeric organophosphates have yielded vital information on their binding orientation in the ground and transition states. (3) Studies in oxime reactivation of inhibited cholinesterase have uncovered the basis for enhanced reactivity of HI-6 compared to 2-PAM. (4) The interactions of fasciculin 2 with acetylcholinesterase have been studied by kinetic and site-specific mutagenesis methods.
- Research Organization:
- California Univ., San Diego, CA (United States)
- OSTI ID:
- 381617
- Report Number(s):
- AD-A-310710/9/XAB; CNN: Contract DAMD17-95-1-5027; TRN: 62750443
- Resource Relation:
- Other Information: PBD: Apr 1996
- Country of Publication:
- United States
- Language:
- English
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