The structure of the segment 1 domain of gelsolin, a protein that frag
ments actin filaments in cells, is reported in complex with actin. Seg
ment 1 binds monomer using an apolar patch rimmed by hydrogen bonds in
a cleft between actin domains. On the actin filament model it binds t
angentially, 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.