Latrunculin alters the actin-monomer subunit interface to prevent polymerization

Nat Cell Biol. 2000 Jun;2(6):376-8. doi: 10.1038/35014075.

Authors

W M Morton¹, K R Ayscough, P J McLaughlin

Affiliation

¹ The Wellcome Trust Centre for Cell Biology, Institute of Cell and Molecular Biology, University of Edinburgh, Swann Building, King's Buildings, Mayfield Road, Edinburgh EH9 3JR, UK.

PMID: 10854330
DOI: 10.1038/35014075

No abstract available

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Actins / chemistry*
Actins / genetics
Actins / metabolism*
Animals
Binding Sites / drug effects
Biopolymers / chemistry
Biopolymers / genetics
Biopolymers / metabolism
Bridged Bicyclo Compounds, Heterocyclic / chemistry*
Bridged Bicyclo Compounds, Heterocyclic / metabolism*
Bridged Bicyclo Compounds, Heterocyclic / pharmacology
Crystallography, X-Ray
Gelsolin / chemistry
Gelsolin / metabolism
Humans
Models, Molecular
Molecular Sequence Data
Mutation / genetics
Porifera / chemistry*
Protein Binding / drug effects
Protein Conformation / drug effects
Thiazoles / chemistry*
Thiazoles / metabolism*
Thiazoles / pharmacology
Thiazolidines
Yeasts / genetics

Substances

Actins
Biopolymers
Bridged Bicyclo Compounds, Heterocyclic
Gelsolin
Thiazoles
Thiazolidines
latrunculin A

Associated data

PDB/1EQY
PDB/1ESV