Models of the actin-bound forms of the β-thymosins

Bo Xue, Adeleke Halilu Aguda, Robert Charles Robinson

Research output: Chapter in Book/Report/Conference proceedingConference contribution

9 Citations (Scopus)


In recent years two structures have been reported that demonstrate how the two halves of a β-thymosin repeat bind to actin monomers. Here we assess the validity of these structures and construct minimally biased models of the β-thymosin:actin complexes. The models reveal that the β-thymosins interact with actin throughout their length and that all the conserved residues are functional in this interface. These models are judged to be in excellent agreement with published biochemical and functional data. In particular, the models are consistent with the actin monomer sequestering and actin filament binding properties of β-thymosins. The models also correctly predict competition between thymosin-β4 with DNase I or profilin in binding actin while allowing ternary complexes at higher concentrations.

Original languageEnglish
Title of host publicationAnnals of the New York Academy of Sciences
PublisherBlackwell Publishing Inc.
Number of pages11
ISBN (Print)1573317012, 9781573317016
Publication statusPublished - Sept 2007
Externally publishedYes

Publication series

NameAnnals of the New York Academy of Sciences
ISSN (Print)0077-8923
ISSN (Electronic)1749-6632


  • Actin
  • Model
  • Structure
  • β-thymosin

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • History and Philosophy of Science


Dive into the research topics of 'Models of the actin-bound forms of the β-thymosins'. Together they form a unique fingerprint.

Cite this