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Calcium‐induced conformational changes in the amino‐terminal half of gelsolin
Author(s) -
Roustan Claude,
Ferjani Imen,
Maciver Sutherland K.,
Fattoum Abdellatif,
Rebière Bertrand,
Benyamin Yves
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.01.031
Subject(s) - gelsolin , calcium , proteolysis , chemistry , actin , context (archaeology) , affinities , biophysics , calcium binding protein , biochemistry , binding site , crystallography , microbiology and biotechnology , biology , enzyme , paleontology , organic chemistry
Gelsolin is an actin‐binding protein that is regulated by the occupancy of multiple calcium‐binding sites. We have studied calcium induced conformational changes in the G1–2 and G1–3 sub‐domains, and report the binding affinities for the three type II sites. A new probe for G3 has been produced and a K d of 5 μM has been measured for calcium in the context of G1–3. The two halves of gelsolin, G1–3 and G4–6 bind weakly with or without calcium, suggesting that once separated by apoptotic proteolysis, G1–3 and G4–6 remain apart allowing G1–3 to sever actin in a calcium free manner.