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High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion.

Authors :
Bollati M
Scalone E
Bonì F
Mastrangelo E
Giorgino T
Milani M
de Rosa M
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2019 Oct 08; Vol. 518 (1), pp. 94-99. Date of Electronic Publication: 2019 Aug 12.
Publication Year :
2019

Abstract

The second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca <superscript>2+</superscript> -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 Cd <superscript>2+</superscript> , in lieu of the physiological calcium. Here, we report the wild type structure of G2 in complex with Ca <superscript>2+</superscript> highlighting subtle ion-dependent differences. Previous findings on different G2 mutations are also briefly revised in light of these results.<br /> (Copyright © 2019 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1090-2104
Volume :
518
Issue :
1
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
31416615
Full Text :
https://doi.org/10.1016/j.bbrc.2019.08.013