Structure of gelsolin segment 1-actin complex and the mechanism of filament severing

Nature. 1993 Aug 19;364(6439):685-92. doi: 10.1038/364685a0.


The structure of the segment 1 domain of gelsolin, a protein that fragments actin filaments in cells, is reported in complex with actin. Segment 1 binds monomer using an apolar patch rimmed by hydrogen bonds in a cleft between actin domains. On the actin filament model it binds tangentially, disrupting only those contacts between adjacent subunits in one helical strand. The segment 1 fold is general for all segments of the gelsolin family because the conserved residues form the core of the structure. It also provides a basis for understanding the origin of an amyloidosis caused by a gelsolin variant.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / chemistry*
  • Actins / metabolism
  • Amino Acid Sequence
  • Amyloidosis / genetics
  • Binding Sites
  • Calcium / chemistry
  • Calcium-Binding Proteins / chemistry*
  • Calcium-Binding Proteins / genetics
  • Calcium-Binding Proteins / metabolism
  • Computer Graphics
  • Gelsolin
  • Humans
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • X-Ray Diffraction


  • Actins
  • Calcium-Binding Proteins
  • Gelsolin
  • Microfilament Proteins
  • Calcium