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Study · Not a test of the peptide alone · 2016

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Utilization of paramagnetic relaxation enhancements for structural analysis of actin-binding proteins in complex with actin.

Huang S, Umemoto R, Tamura Y, Kofuku Y, Uyeda TQ, Nishida N, Shimada I

Scientific reports22 Sept 2016Cited by 9 (Europe PMC)

PMID27654858 (opens in a new tab)PMCIDPMC5031973 (opens in a new tab)DOI10.1038/srep33690 (opens in a new tab)PepBankPUB-27654858
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Summary

Actin cytoskeleton dynamics are controlled by various actin binding proteins (ABPs) that modulate the polymerization of the monomeric G-actin and the depolymerization of filamentous F-actin. Although revealing the structures of the actin/ABP complexes is crucial to understand how the ABPs regulate actin dynamics, the X-ray crystallography and cryoEM methods are inadequate to apply for the ABPs that interact with G- or F-actin with lower affinity or multiple binding modes. In this study, we aimed to establish the alternative method to build a structural model of G-actin/ABP complexes, utilizing the paramagnetic relaxation enhancement (PRE) experiments. Thymosin β4 (Tβ4) was used as a test case for validation, since its structure in complex with G-actin was reported recently. Recombinantly expressed G-actin, containing a cysteine mutation, was conjugated with a nitroxyl spin label at the specific site. Based on the intensity ratio of the 1H-15N HSQC spectra of Tβ4 in the complex with G-actin in the paramagnetic and diamagnetic states, the distances between the amide groups of Tβ4 and the spin label of G-actin were estimated. Using the PRE-derived distance constraints, we were able to compute a well-converged docking structure of the G-actin/Tβ4 complex that shows great accordance with the reference structure.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study1

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

Studies that did not test the peptide alone1

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)Other

    Paramagnetic relaxation enhancement distance constraints gave a well-converged docking structure of the G-actin/Tβ4 complex that agreed with the reference structure.

    In plain wordsIn lab tests, a structural method built a model of Tβ4 bound to actin that matched the known structure.

    Peptide
    Thymosin beta-4 (human)
    Outcome
    Not applicablePRE-derived docking structure of the G-actin/Tβ4 complex
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Using the PRE-derived distance constraints, we were able to compute a well-converged docking structure of the G-actin/Tβ4 complex that shows great accordance with the reference structure.
    1 context sentence
    Summary · context
    Thymosin β4 (Tβ4) was used as a test case for validation, since its structure in complex with G-actin was reported recently.

    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.

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