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Search: WFRF:(Schutt CE)

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  • Chumnarnsilpa, Sakesit, 1967-, et al. (author)
  • Activation in isolation : exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin
  • 2003
  • In: FEBS Letters. - Netherlands : Elsevier Science B.V.. - 0014-5793 .- 1873-3468. ; 552:2-3, s. 82-85
  • Journal article (peer-reviewed)abstract
    • Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 A resolution in the presence of Ca(2+) ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca(2+) sites occupied. Neither actin nor the type-l Ca(2+), which normally is sandwiched between actin and G4, is required to achieve this conformation.
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