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

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

P J McLaughlin  1 , J T Gooch, H G Mannherz, A G Weeds
Affiliations

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

P J McLaughlin et al. Nature. .

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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