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

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

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          Abstract

          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.

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