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Study · Not a test of the peptide alone · 2004

3 results

Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance.

Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C

The Journal of biological chemistry22 Mar 2004Cited by 75 (Europe PMC)

PMID15039431 (opens in a new tab)DOI10.1074/jbc.m311413200 (opens in a new tab)PepBankPUB-15039431
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Summary

Thymosin beta4 is a major actin-sequestering protein, yet the structural basis for its biological function is still unknown. This study provides insight regarding the way this 43-amino acid peptide, mostly unstructured in solution, binds to monomeric actin and prevents its assembly in filaments. We show here that the whole backbone of thymosin beta4 is highly affected upon binding to G-actin. The assignment of all amide protons and nitrogens of thymosin in the bound state, obtained using a combination of NMR experiments and selective labelings, shows that thymosin folds completely upon binding and displays a central extended region flanked by two N- and C-terminal helices. The cleavage of actin by subtilisin in the DNase I binding loop does not modify the structure of thymosin beta4 in the complex, showing that the backbone of the peptide is not in close proximity to segment 42-47 of actin. The combination of our NMR results and previously published mutation and cross-link data allows a better characterization of the binding mode of thymosins on G-actin.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study3

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone3

In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Thymosin beta-4 (human).

  1. 01LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism

    In NMR experiments, the whole backbone of thymosin beta4 was highly affected upon binding to G-actin.

    In plain wordsIn lab tests, the whole backbone of thymosin beta4 changed when it bound to G-actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableBackbone changes on binding to G-actin
    Study

    n: not reported in source

    NMR of thymosin beta4 bound to monomeric actin
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    We show here that the whole backbone of thymosin beta4 is highly affected upon binding to G-actin.

    In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).

  2. 02LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism

    In NMR experiments, thymosin folded completely upon binding to actin, with a central extended region flanked by two N- and C-terminal helices.

    In plain wordsIn lab tests, thymosin beta4 folded fully when bound to actin, with a central stretch between two helices.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableFolding of thymosin beta4 upon binding
    Study

    n: not reported in source

    NMR of thymosin beta4 bound to monomeric actin
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    shows that thymosin folds completely upon binding and displays a central extended region flanked by two N- and C-terminal helices.

    In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).

  3. 03LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism

    Cleavage of actin by subtilisin in the DNase I binding loop did not modify the structure of thymosin beta4 in the complex.

    In plain wordsIn lab tests, cutting actin at one loop did not change the structure of thymosin beta4 bound to it.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    No significant changeEffect of actin cleavage on thymosin beta4 structure in the complex
    Study

    n: not reported in source

    NMR of thymosin beta4 bound to monomeric actin
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The cleavage of actin by subtilisin in the DNase I binding loop does not modify the structure of thymosin beta4 in the complex, showing that the backbone of the peptide is not in close proximity to segment 42-47 of actin.

    In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    13 Oct 2026, 01:52 UTC

    Study results updated

  2. Version 1

    12 Oct 2026, 18:17 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

Publication types

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