6qw3

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Calcium-bound gelsolin domain 2

Structural highlights

6qw3 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.3Å
Ligands:CA
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

The 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.

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Citations
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A novel hotspot of gelsolin instability triggers an alternative mechanism of amyloid aggregation.
Bollati et al. (2021)
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See Also

References

  1. ↑ Haltia M, Prelli F, Ghiso J, Kiuru S, Somer H, Palo J, Frangione B. Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein. Biochem Biophys Res Commun. 1990 Mar 30;167(3):927-32. PMID:2157434
  2. ↑ Maury CP, Alli K, Baumann M. Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline. FEBS Lett. 1990 Jan 15;260(1):85-7. PMID:2153578
  3. ↑ Ghiso J, Haltia M, Prelli F, Novello J, Frangione B. Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type. Biochem J. 1990 Dec 15;272(3):827-30. PMID:2176481
  4. ↑ de la Chapelle A, Tolvanen R, Boysen G, Santavy J, Bleeker-Wagemakers L, Maury CP, Kere J. Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187. Nat Genet. 1992 Oct;2(2):157-60. PMID:1338910 doi:http://dx.doi.org/10.1038/ng1092-157
  5. ↑ Kim J, Lee JE, Heynen-Genel S, Suyama E, Ono K, Lee K, Ideker T, Aza-Blanc P, Gleeson JG. Functional genomic screen for modulators of ciliogenesis and cilium length. Nature. 2010 Apr 15;464(7291):1048-51. doi: 10.1038/nature08895. PMID:20393563 doi:10.1038/nature08895
  6. ↑ 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. 2019 Aug 12. pii: S0006-291X(19)31515-3. doi:, 10.1016/j.bbrc.2019.08.013. PMID:31416615 doi:http://dx.doi.org/10.1016/j.bbrc.2019.08.013

Contents


PDB ID 6qw3

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OCA

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