Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity

Angew Chem Int Ed Engl. 2013 Jan 7;52(2):562-7. doi: 10.1002/anie.201206561. Epub 2012 Nov 12.

Abstract

Aggravating aggregation: an N-terminal domain that is in close proximity to the polyQ domain in the huntingtin protein, htt105-138, is shown to be highly aggregation prone. Potential cross-talk between this domain and the polyQ region may play a central role in regulating the aggregation and toxicity of Htt-N-terminal fragments.

MeSH terms

  • Amino Acid Sequence
  • Humans
  • Huntingtin Protein
  • Huntington Disease / genetics
  • Huntington Disease / metabolism*
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Protein Structure, Tertiary

Substances

  • HTT protein, human
  • Huntingtin Protein
  • Nerve Tissue Proteins