Cholinesterase Structure: Identification of Residues and Domains Affecting Organophosphate Inhibition and Catalysis.

Abstract

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.

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Document Details

Document Type
Technical Report
Publication Date
Apr 01, 1996
Accession Number
ADA310710

Entities

People

  • Palmer W. Taylor

Organizations

  • University of California, San Diego

Tags

Communities of Interest

  • Biomedical
  • Energy and Power Technologies
  • Weapons Technologies

DTIC Thesaurus Topics

  • Amines
  • Cells
  • Chemical Synthesis
  • Chemistry
  • Crystal Structure
  • Enzyme Inhibitors
  • Fish
  • Fungi
  • Health Services
  • Molecular Dynamics
  • Organic Chemistry

Fields of Study

  • Chemistry

Readers

  • Molecular Genetics
  • Neurotoxicology
  • Systems Analysis and Design