Influence of the N terminus and the actin-binding motif of thymosin beta4 on its interaction with G-actin.

@article{Zoubek2007InfluenceOT,
  title={Influence of the N terminus and the actin-binding motif of thymosin beta4 on its interaction with G-actin.},
  author={Robert E Zoubek and Ewald Hannappel},
  journal={Annals of the New York Academy of Sciences},
  year={2007},
  volume={1112},
  pages={435-41}
}
Thymosin beta(4) binds G-actin in a 1:1 ratio and prevents its aggregation to F-actin by sequestration. Substitution or modification of single amino acid residues within the N-terminal sequence 1 to 22 of thymosin beta(4) alters its interaction with G-actin. We generated thymosin beta(4) variants with amino acid substitutions within the N-terminal alpha-helix and the putative actin-binding motif. None of the E. coli-generated thymosin beta(4) variants was modified or acetylated at its N… CONTINUE READING