Key result
Thymosin beta4 folds completely upon binding to G-actin, displaying a central extended region flanked by two N- and C-terminal helices, as determined by NMR.
Population
Thymosin beta4 and monomeric actin (G-actin)
Design
Preclinical
Authors
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No immediate clinical implications; leaves open whether this actin-binding structure informs cardiovascular therapies.
This study elucidates the structural basis of thymosin beta4 binding to G-actin, showing that the mostly unstructured peptide folds completely upon binding.
Domanski et al. (2004) studied this question. Thymosin beta4 interaction with monomeric actin was evaluated on Structural changes upon binding to G-actin. Thymosin beta4 folds completely upon binding to G-actin, displaying a central extended region flanked by two N- and C-terminal helices, as determined by NMR.
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