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|Title:||Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins||Authors:||Xue, B.
Robinson, Robert Charles
|Issue Date:||2016||Source:||Xue, B., & Robinson, R. C. (2016). Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins. Vitamins and Hormones, 102, 55-71.||Series/Report no.:||Vitamins and Hormones||Abstract:||Thymosin β4 (Tβ4) is a 43-amino acid signature motif peptide that defines the beta-thymosin (βT) family of proteins. βTs are intrinsically unstructured in their free states and undergo disorder-to-order transitions in carrying out their biological functions. This property poses challenges in determining their 3D structures, mainly favoring structural studies on the complexes formed between βTs and their interaction partners. One of the βTs’ primary binding partners is monomeric actin, a major component of the cytoskeleton in eukaryotic cells. Tβ4’s role in this system is to maintain the highly concentrated pool of monomeric actin that can be accessed through profilin by actin filament nucleating machineries. Here, we give an account of the structures of βTs that have been illuminated by nuclear magnetic resonance (NMR) and X-ray crystallography. NMR has been the method of choice for probing regions that have intrinsic conformational preference within the largely disordered βTs in their native states in solution. X-ray crystallography has demonstrated at atomic detail how βTs interact with actin. Detailed analysis of these structures highlights the disorder-to-order transition of Tβ4 in binding to actin and its isoform specificity.||URI:||https://hdl.handle.net/10356/83977
|ISSN:||0083-6729||DOI:||10.1016/bs.vh.2016.04.007||Rights:||© 2016 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Vitamins and Hormones, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1016/bs.vh.2016.04.007].||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Journal Articles|
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