STRUCTURE OF GELSOLIN SEGMENT-1-ACTIN COMPLEX AND THE MECHANISM OF FILAMENT SEVERING

Citation
Pj. Mclaughlin et al., STRUCTURE OF GELSOLIN SEGMENT-1-ACTIN COMPLEX AND THE MECHANISM OF FILAMENT SEVERING, Nature, 364(6439), 1993, pp. 685-692
Citations number
46
Categorie Soggetti
Multidisciplinary Sciences
Journal title
NatureACNP
ISSN journal
00280836
Volume
364
Issue
6439
Year of publication
1993
Pages
685 - 692
Database
ISI
SICI code
0028-0836(1993)364:6439<685:SOGSCA>2.0.ZU;2-V
Abstract
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.