Structure solution of misfolded conformations adopted by intrinsically disordered Alzheimer's tau protein

Protein Pept Lett. 2009;16(1):61-4. doi: 10.2174/092986609787049349.

Abstract

Until now it was impossible to obtain atomic structure of intrinsically disordered protein (IDP) tau and/or its assembly in Alzheimer's paired helical filaments as neither of them could have been prepared in the form amenable to X-ray or NMR techniques. Using IDP tau property to attain regular tertiary structure after binding events during self-assembly or when complexed with its target we propose monoclonal antibodies as surrogate tau protein binding partners to form complexes and crystals for structure solution by X-ray technique.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal
  • Protein Conformation*
  • Protein Folding
  • tau Proteins / chemistry*
  • tau Proteins / immunology

Substances

  • Antibodies, Monoclonal
  • tau Proteins