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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McLaughlin, P., Gooch, J., Mannherz, HG. et al. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364, 685–692 (1993). https://doi.org/10.1038/364685a0
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DOI: https://doi.org/10.1038/364685a0
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