Please use this identifier to cite or link to this item: https://doi.org/10.1038/srep45230
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dc.titleStructural Basis for pH-mediated Regulation of F-actin Severing by Gelsolin Domain 1
dc.contributor.authorFan J.-S.
dc.contributor.authorGoh H.
dc.contributor.authorDIng K.
dc.contributor.authorXue B.
dc.contributor.authorRobinson R.C.
dc.contributor.authorYang D.
dc.date.accessioned2020-09-09T05:07:06Z
dc.date.available2020-09-09T05:07:06Z
dc.date.issued2017
dc.identifier.citationFan J.-S., Goh H., DIng K., Xue B., Robinson R.C., Yang D. (2017). Structural Basis for pH-mediated Regulation of F-actin Severing by Gelsolin Domain 1. Scientific Reports 7 : 45230. ScholarBank@NUS Repository. https://doi.org/10.1038/srep45230
dc.identifier.issn20452322
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/175217
dc.description.abstractSix-domain gelsolin regulates actin structural dynamics through its abilities to sever, cap and uncap F-actin. These activities are modulated by various cellular parameters like Ca2+ and pH. Until now, only the molecular activation mechanism of gelsolin by Ca2+ has been understood relatively well. The fragment comprising the first domain and six residues from the linker region into the second domain has been shown to be similar to the full-length protein in F-actin severing activity in the absence of Ca2+ at pH 5. To understand how this gelsolin fragment is activated for F-actin severing by lowering pH, we solved its NMR structures at both pH 7.3 and 5 in the absence of Ca2+ and measured the pKa values of acidic amino acid residues and histidine residues. The overall structure and dynamics of the fragment are not affected significantly by pH. Nevertheless, local structural changes caused by protonation of His29 and Asp109 result in the activation on lowering the pH, and protonation of His151 directly effects filament binding since it resides in the gelsolin/actin interface. Mutagenesis studies support that His29, Asp109 and His151 play important roles in the pH-dependent severing activity of the gelsolin fragment. © 2017 The Author(s).
dc.sourceUnpaywall 20200831
dc.subjectactin
dc.subjectcalcium
dc.subjectgelsolin
dc.subjectprotein binding
dc.subjectbinding site
dc.subjectchemistry
dc.subjecthuman
dc.subjectmetabolism
dc.subjectmolecular docking
dc.subjectpH
dc.subjectActins
dc.subjectBinding Sites
dc.subjectCalcium
dc.subjectGelsolin
dc.subjectHumans
dc.subjectHydrogen-Ion Concentration
dc.subjectMolecular Docking Simulation
dc.subjectProtein Binding
dc.typeArticle
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.contributor.departmentDEPT OF BIOCHEMISTRY
dc.description.doi10.1038/srep45230
dc.description.sourcetitleScientific Reports
dc.description.volume7
dc.description.page45230
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