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Study · In vitro (cell-free) · 2014

3 results

Structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization.

Xue B, Leyrat C, Grimes JM, Robinson RC

Proceedings of the National Academy of Sciences of the United States of America13 Oct 2014Cited by 76 (Europe PMC)

PMID25313062 (opens in a new tab)PMCIDPMC4217450 (opens in a new tab)DOI10.1073/pnas.1412271111 (opens in a new tab)PepBankPUB-25313062
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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 study3

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

  1. 01LabIn vitro (cell-free)Mechanism

    In a Tβ4:actin structure, Tβ4 has two helices that bind at the barbed and pointed faces of G-actin and prevent incorporation of the bound G-actin into a filament.

    In plain wordsIn lab tests, thymosin beta‑4 binds actin at two sites and keeps it from joining an actin filament.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableBinding of Tβ4 to G-actin
    Study

    n: not reported in source

    Tβ4:actin crystal structures
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The first structure shows that Tβ4 has two helices that bind at the barbed and pointed faces of G-actin, preventing the incorporation of the bound G-actin into a filament.
    1 context sentence
    Summary · context
    Here, we report two Tβ4:actin structures.
  2. 02LabIn vitro (cell-free)Mechanism

    A second Tβ4:actin structure shows a more open nucleotide binding cleft on G-actin, typical of profilin:actin, with disruption of the Tβ4 C-terminal helix interaction.

    In plain wordsIn lab tests, a second structure showed actin in a more open state, with part of thymosin beta‑4's binding disrupted.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableTβ4:actin structure with open nucleotide binding cleft
    Study

    n: not reported in source

    Tβ4:actin crystal structures
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The second structure displays a more open nucleotide binding cleft on G-actin, which is typical of profilin:actin structures, with a concomitant disruption of the Tβ4 C-terminal helix interaction.
    1 context sentence
    Summary · context
    Here, we report two Tβ4:actin structures.
  3. 03LabIn vitro (cell-free)Mechanism

    Structures, biochemical assays and molecular dynamics simulations show that exchange of bound actin between Tβ4 and profilin involves steric and allosteric components.

    In plain wordsIn lab tests, passing actin between thymosin beta‑4 and profilin involves both physical blocking and shape changes in actin.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicableExchange of actin between Tβ4 and profilin
    Study

    n: not reported in source

    Tβ4:actin crystal structures
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    These structures, combined with biochemical assays and molecular dynamics simulations, show that the exchange of bound actin between Tβ4 and profilin involves both steric and allosteric components.
    1 context sentence
    Summary · context
    Here, we report two Tβ4:actin structures.

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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