Molecular modeling of the collagen-like tail of asymmetric acetylcholinesterase

Protein Eng. 2000 Jan;13(1):27-34. doi: 10.1093/protein/13.1.27.

Abstract

The asymmetric form of acetylcholinesterase comprises three catalytic tetramers attached to ColQ, a collagen-like tail responsible for the anchorage of the enzyme to the synaptic basal lamina. ColQ is composed of an N-terminal domain which interacts with the catalytic subunits of the enzyme, a central collagen-like domain and a C-terminal globular domain. In particular, the collagen-like domain of ColQ contains two heparin-binding domains which interact with heparan sulfate proteoglycans in the basal lamina. A three-dimensional model of the collagen-like domain of the tail of asymmetric acetylcholinesterase was constructed. The model presents an undulated shape that results from the presence of a substitution and an insertion in the Gly-X-Y repeating pattern, as well as from low imino-acid regions. Moreover, this model permits the analysis of interactions between the heparin-binding domains of ColQ and heparin, and could also prove useful in the prediction of interaction domains with other putative basal lamina receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / chemistry*
  • Acetylcholinesterase / metabolism
  • Amino Acid Sequence
  • Binding Sites
  • Collagen / chemistry*
  • Heparin / metabolism
  • Models, Molecular*
  • Molecular Sequence Data
  • Protein Conformation

Substances

  • Heparin
  • Collagen
  • Acetylcholinesterase