Loss of a metal-binding site in gelsolin leads to familial amyloidosis–Finnish type

@article{Kazmirski2002LossOA,
  title={Loss of a metal-binding site in gelsolin leads to familial amyloidosis–Finnish type},
  author={Steven L. Kazmirski and Rivka L Isaacson and Chahm An and Ashley M. Buckle and Christopher Mark Johnson and Valerie Daggett and A. R. Fersht},
  journal={Nature Structural Biology},
  year={2002},
  volume={9},
  pages={112-116}
}
Mutations in domain 2 (D2, residues 151–266) of the actin-binding protein gelsolin cause familial amyloidosis–Finnish type (FAF). These mutations, D187N or D187Y, lead to abnormal proteolysis of plasma gelsolin at residues 172–173 and a second hydrolysis at residue 243, resulting in an amyloidogenic fragment. Here we present the structure of human gelsolin D2 at 1.65 Å and find that Asp 187 is part of a Cd2+ metal-binding site. Two Ca2+ ions are required for a conformational transition of… CONTINUE READING
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