Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins
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 determi...
| Main Authors: | , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
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2016
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| Online Access: | https://hdl.handle.net/10356/83977 http://hdl.handle.net/10220/41562 |
| _version_ | 1811696045594247168 |
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| author | Xue, B. Robinson, Robert Charles |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Xue, B. Robinson, Robert Charles |
| author_sort | Xue, B. |
| collection | NTU |
| description | 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. |
| first_indexed | 2024-10-01T07:33:07Z |
| format | Journal Article |
| id | ntu-10356/83977 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:33:07Z |
| publishDate | 2016 |
| record_format | dspace |
| spelling | ntu-10356/839772023-02-28T17:04:17Z Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins Xue, B. Robinson, Robert Charles School of Biological Sciences Institute of Structural Biology beta-thymosin thymosin β4 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. ASTAR (Agency for Sci., Tech. and Research, S’pore) Accepted version 2016-10-10T08:50:28Z 2019-12-06T15:35:43Z 2016-10-10T08:50:28Z 2019-12-06T15:35:43Z 2016 Journal Article Xue, B., & Robinson, R. C. (2016). Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins. Vitamins and Hormones, 102, 55-71. 0083-6729 https://hdl.handle.net/10356/83977 http://hdl.handle.net/10220/41562 10.1016/bs.vh.2016.04.007 en Vitamins and Hormones © 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]. 15 p. application/pdf |
| spellingShingle | beta-thymosin thymosin β4 Xue, B. Robinson, Robert Charles Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins |
| title | Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins |
| title_full | Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins |
| title_fullStr | Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins |
| title_full_unstemmed | Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins |
| title_short | Actin-Induced Structure in the Beta-Thymosin Family of Intrinsically Disordered Proteins |
| title_sort | actin induced structure in the beta thymosin family of intrinsically disordered proteins |
| topic | beta-thymosin thymosin β4 |
| url | https://hdl.handle.net/10356/83977 http://hdl.handle.net/10220/41562 |
| work_keys_str_mv | AT xueb actininducedstructureinthebetathymosinfamilyofintrinsicallydisorderedproteins AT robinsonrobertcharles actininducedstructureinthebetathymosinfamilyofintrinsicallydisorderedproteins |