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

Article Details

Citation

McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG

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

Nature. 1993 Aug 19;364(6439):685-92.

PubMed ID
8395021 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
GelsolinP06396Details