Article
Mutations in actin used for structural studies partially disrupt β-thymosin/WH2 domains interaction.
FEBS letters - 1 Oct 2016
Deville Célia, Girard-Blanc Christine, Assrir Nadine, Nhiri Naïma, Jacquet Eric, Bontems François, Renault Louis, Petres Stéphane, van Heijenoort Carine
Abstract excerpt
Understanding the structural basis of actin cytoskeleton remodeling requires stabilization of actin monomers, oligomers, and filaments in complex with partner proteins, using various biochemical strategies. Here, we report a dramatic destabilization of the dynamic interaction with a model β-thymosin/WH2 domain induced by mutations in actin. This result underlines that mutant actins should be used with prudence to...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
