| Literature DB >> 31416615 |
Michela Bollati1, Emanuele Scalone1, Francesco Bonì1, Eloise Mastrangelo1, Toni Giorgino1, Mario Milani1, Matteo de Rosa2.
Abstract
The second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca2+-bound; it is also a dynamic protein, hence structural biologists often rely on the study of the isolated G2. However, the wild type G2 structure that have been used so far in comparative studies is bound to a crystallographic Cd2+, in lieu of the physiological calcium. Here, we report the wild type structure of G2 in complex with Ca2+ highlighting subtle ion-dependent differences. Previous findings on different G2 mutations are also briefly revised in light of these results.Entities:
Keywords: AGel amyloidosis; Calcium; Gelsolin; Pathogenic mutations; X-ray crystallography
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Year: 2019 PMID: 31416615 DOI: 10.1016/j.bbrc.2019.08.013
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575