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PMID: 8395021 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

Nature ·Vol. 364 ·No. 6439 ·1993-08-19 ·Pages 685-92

McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG

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.

MeSH Terms
Actins/chemistry,metabolism Amino Acid Sequence Amyloidosis/genetics Binding Sites Calcium/chemistry Calcium-Binding Proteins/chemistry,genetics,metabolism Computer Graphics Gelsolin Humans Microfilament Proteins/chemistry,genetics,metabolism Models, Molecular Molecular Sequence Data Protein Conformation X-Ray Diffraction
Chemicals
Actins Calcium-Binding Proteins Gelsolin Microfilament Proteins Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
McLaughlin P J
MRC Laboratory of Molecular Biology, Cambridge, UK.
Gooch J T
Mannherz H G
Weeds A G
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1993-08-19
Pages
685-92
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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