Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Citations (Scopus)

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.

Original languageEnglish
Title of host publicationThymosins, 2016
EditorsGerald Litwack
PublisherAcademic Press Inc.
Pages55-71
Number of pages17
ISBN (Print)9780128048184
DOIs
Publication statusPublished - Jan 1 2016
Externally publishedYes

Publication series

NameVitamins and Hormones
Volume102
ISSN (Print)0083-6729

Fingerprint

Intrinsically Disordered Proteins
Thymosin
Actins
X Ray Crystallography
Magnetic Resonance Spectroscopy
Profilins
Amino Acid Motifs
Eukaryotic Cells
Cytoskeleton
Actin Cytoskeleton
Protein Isoforms
Peptides
Proteins

Keywords

  • Actin
  • Beta-thymosin
  • Crystallography
  • Intrinsically disordered/unstructured proteins
  • NMR
  • Protein hybrid
  • Structure
  • Thymosin β4

ASJC Scopus subject areas

  • Physiology
  • Endocrinology

Cite this

Xue, B., & Robinson, R. C. (2016). Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins. In G. Litwack (Ed.), Thymosins, 2016 (pp. 55-71). (Vitamins and Hormones; Vol. 102). Academic Press Inc.. https://doi.org/10.1016/bs.vh.2016.04.007

Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins. / Xue, B.; Robinson, R. C.

Thymosins, 2016. ed. / Gerald Litwack. Academic Press Inc., 2016. p. 55-71 (Vitamins and Hormones; Vol. 102).

Research output: Chapter in Book/Report/Conference proceedingChapter

Xue, B & Robinson, RC 2016, Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins. in G Litwack (ed.), Thymosins, 2016. Vitamins and Hormones, vol. 102, Academic Press Inc., pp. 55-71. https://doi.org/10.1016/bs.vh.2016.04.007
Xue B, Robinson RC. Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins. In Litwack G, editor, Thymosins, 2016. Academic Press Inc. 2016. p. 55-71. (Vitamins and Hormones). https://doi.org/10.1016/bs.vh.2016.04.007
Xue, B. ; Robinson, R. C. / Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins. Thymosins, 2016. editor / Gerald Litwack. Academic Press Inc., 2016. pp. 55-71 (Vitamins and Hormones).
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