6qw3
From Proteopedia
Calcium-bound gelsolin domain 2
Structural highlights
Disease[GELS_HUMAN] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:105120]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.[1] [2] [3] [4] Function[GELS_HUMAN] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.[5] Publication Abstract from PubMedThe second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca(2+)-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(2+), in lieu of the physiological calcium. Here, we report the wild type structure of G2 in complex with Ca(2+) highlighting subtle ion-dependent differences. Previous findings on different G2 mutations are also briefly revised in light of these results. High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion.,Bollati M, Scalone E, Boni F, Mastrangelo E, Giorgino T, Milani M, de Rosa M Biochem Biophys Res Commun. 2019 Aug 12. pii: S0006-291X(19)31515-3. doi:, 10.1016/j.bbrc.2019.08.013. PMID:31416615[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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