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Study · In vitro (cell-free) · 1996

5 results

The actin binding site of thymosin beta 4 mapped by mutational analysis.

Van Troys M, Dewitte D, Goethals M, Carlier MF, Vandekerckhove J, Ampe C

The EMBO journal1 Jan 1996Cited by 93 (Europe PMC)

PMID8617195 (opens in a new tab)DOI10.1002/j.1460-2075.1996.tb00350.x (opens in a new tab)PepBankPUB-08617195
Publisher pagePubMedAsk about this study
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study5

5 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cell-free)Mechanism

    The N-terminal part (residues 1-16) and a hexapeptide motif (residues 17-22) of thymosin beta‑4 form separate structural entities.

    In plain wordsIn lab tests, thymosin beta‑4 has two separate parts that take part in actin binding.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableStructure of the actin binding site of thymosin beta 4
    Study

    n: not reported in source

    synthetic peptide variants and purified actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The N-terminal part (residues 1-16) and a hexapeptide motif (residues 17-22) form separate structural entities.
    2 context sentences
    Summary · context
    We characterized in detail the actin binding site of the small actin-sequestering protein thymosin beta 4 (T beta 4) using chemically synthesized full-length T beta 4 variants.
    Summary · context
    In both, we identified charged and hydrophobic residues that participate in the actin interaction using chemical cross-linking, complex formation in native gels and actin-sequestering experiments.
  2. 02LabIn vitro (cell-free)Activity measurement

    Charged and hydrophobic residues of thymosin beta‑4 take part in the actin interaction, as shown by cross-linking, native gels and actin-sequestering experiments.

    In plain wordsIn lab tests, both charged and water-avoiding parts of thymosin beta‑4 helped it contact actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableResidues of thymosin beta 4 that take part in actin interaction
    Study

    n: not reported in source

    synthetic peptide variants and purified actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In both, we identified charged and hydrophobic residues that participate in the actin interaction using chemical cross-linking, complex formation in native gels and actin-sequestering experiments.
    1 context sentence
    Summary · context
    We characterized in detail the actin binding site of the small actin-sequestering protein thymosin beta 4 (T beta 4) using chemically synthesized full-length T beta 4 variants.
  3. 03LabIn vitro (cell-free)Mechanism

    A model is proposed in which the N-terminal part of thymosin beta‑4 adopts an alpha-helix and binds actin through a patch of hydrophobic residues (6M-I-F12).

    In plain wordsIn lab tests, a model suggests the start of thymosin beta‑4 forms a helix to bind actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableAlpha-helix model of N-terminal binding
    Study

    n: not reported in source

    synthetic peptide variants and purified actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Quantitative data on the activity of the variants and circular dichroism experiments allow to present a model in which the N-terminal part needs to adopt an alpha-helix for actin binding and interacts through a patch of hydrophobic residues (6M-I-F12) on one side of this helix.
    2 context sentences
    Summary · context
    We characterized in detail the actin binding site of the small actin-sequestering protein thymosin beta 4 (T beta 4) using chemically synthesized full-length T beta 4 variants.
    Summary · context
    In both, we identified charged and hydrophobic residues that participate in the actin interaction using chemical cross-linking, complex formation in native gels and actin-sequestering experiments.
  4. 04LabIn vitro (cell-free)Mechanism

    Electrostatic contacts between actin and lysine residues 18 and 14 of thymosin beta‑4 appear important for binding.

    In plain wordsIn lab tests, two lysine parts of thymosin beta‑4 seemed important for binding actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableElectrostatic contacts of lysine residues 14 and 18 with actin
    Study

    n: not reported in source

    synthetic peptide variants and purified actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Also, electrostatic contacts between actin and lysine residues 18, in the motif, and 14, in the N-terminal alpha-helix, appear important for binding.
    2 context sentences
    Summary · context
    We characterized in detail the actin binding site of the small actin-sequestering protein thymosin beta 4 (T beta 4) using chemically synthesized full-length T beta 4 variants.
    Summary · context
    In both, we identified charged and hydrophobic residues that participate in the actin interaction using chemical cross-linking, complex formation in native gels and actin-sequestering experiments.
  5. 05LabIn vitro (cell-free)Other

    The residues critical for contacting actin are conserved throughout the beta-thymosin family, and a similar pattern is found in the C-terminal headpiece of villin and dematin.

    In plain wordsIn lab analysis, the actin-contact parts of thymosin beta‑4 are the same across related thymosins and appear in two other proteins.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableConservation of critical residues across the beta-thymosin family
    Study

    n: not reported in source

    synthetic peptide variants and purified actin
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The residues critical for contacting actin are conserved throughout the beta-thymosin family and in addition to this we identify a similar pattern in the C-terminal headpiece of villin and dematin.
    2 context sentences
    Summary · context
    We characterized in detail the actin binding site of the small actin-sequestering protein thymosin beta 4 (T beta 4) using chemically synthesized full-length T beta 4 variants.
    Summary · context
    In both, we identified charged and hydrophobic residues that participate in the actin interaction using chemical cross-linking, complex formation in native gels and actin-sequestering experiments.

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.

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