 |
PDBsum entry 6qw3
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Structural protein
|
PDB id
|
|
|
|
6qw3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
Biochem Biophys Res Commun
518:94-99
(2019)
|
|
PubMed id:
|
|
|
|
|
| |
|
High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion.
|
|
M.Bollati,
E.Scalone,
F.Bonì,
E.Mastrangelo,
T.Giorgino,
M.Milani,
M.de Rosa.
|
|
|
|
| |
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.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
');
}
}
 |