6QW3

Calcium-bound gelsolin domain 2

Summary for 6QW3

• Entry DOI: 10.2210/pdb6qw3/pdb
• Descriptor: Gelsolin, CALCIUM ION (3 entities in total)
• Functional Keywords: amyloidosis, gelsolin, actin-binding, structural protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 13206.73

Authors

Scalone, E.,Boni, F.,Milani, M.,Mastrangelo, E.,de Rosa, M. (deposition date: 2019-03-05, release date: 2019-08-28, Last modification date: 2024-11-13)

Primary citation

Bollati, M.,Scalone, E.,Boni, F.,Mastrangelo, E.,Giorgino, T.,Milani, M.,de Rosa, M.
High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion.
Biochem.Biophys.Res.Commun., 518:94-99, 2019

PubMed Abstract: The second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca-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, in lieu of the physiological calcium. Here, we report the wild type structure of G2 in complex with Ca highlighting subtle ion-dependent differences. Previous findings on different G2 mutations are also briefly revised in light of these results.

PubMed: 31416615
DOI: 10.1016/j.bbrc.2019.08.013

Experimental method

X-RAY DIFFRACTION (1.3 Å)