ArticleScientific reports2016
Utilization of paramagnetic relaxation enhancements for structural analysis of actin-binding proteins in complex with actin.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Characterization of the High-Affinity Fuzzy Complex between the Disordered Domain of the E7 Oncoprotein from High-Risk HPV and the TAZ2 Domain of CBP.Biochemistry · 2021Article
- NMR as a "Gold Standard" Method in Drug Design and Discovery.Molecules (Basel, Switzerland) · 2020Review
- Pick-ya actin - a method to purify actin isoforms with bespoke key post-translational modifications.Journal of cell science · 2020Article
- Metal-Ligand Recognition Index Determination by NMR Proton Relaxation Study.Molecules (Basel, Switzerland) · 2019Article
- GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures.Nature reviews. Drug discovery · 2019Review
- Rapid production of pure recombinant actin isoforms inJournal of cell science · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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
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Registered trials
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