Optimal Mutant Model of Human S100A3 Protein Citrullinated at Arg51 by Peptidylarginine Deiminase Type III and Its Solution Structural Properties.

ABSTRACT: S100A3 protein, a member of the EF-hand-type Ca²⁺-binding S100 protein family, undergoes a Ca²⁺-/Zn²⁺-induced structural change to a tetrameric state upon specific citrullination of R51 in human hair cuticular cells. To elucidate the underlying mechanism, we prepared recombinant mutant S100A3 proteins, including R51A, R51C, R51E, R51K, and R51Q, as potential models of post-translationally modified S100A3 and evaluated their biophysical and biochemical properties relative to wild-type (WT) S100A3 and WT citrullinated in vitro. Size exclusion chromatography (SEC) showed that R51Q formed a tetramer in the presence of Ca²⁺, while Ca²⁺ titration monitored by Trp fluorescence indicated that R51Q had Ca²⁺-binding properties similar

SUBMITTER: Ite K 

PROVIDER: S-EPMC7057681 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature