Ontology highlight
ABSTRACT:
SUBMITTER: Millard TH
PROVIDER: S-EPMC545821 | biostudies-literature | 2005 Jan
REPOSITORIES: biostudies-literature
Millard Thomas H TH Bompard Guillaume G Heung Man Yeung MY Dafforn Timothy R TR Scott David J DJ Machesky Laura M LM Fütterer Klaus K
The EMBO journal 20050106 2
The scaffolding protein insulin receptor tyrosine kinase substrate p53 (IRSp53), a ubiquitous regulator of the actin cytoskeleton, mediates filopodia formation under the control of Rho-family GTPases. IRSp53 comprises a central SH3 domain, which binds to proline-rich regions of a wide range of actin regulators, and a conserved N-terminal IRSp53/MIM homology domain (IMD) that harbours F-actin-bundling activity. Here, we present the crystal structure of this novel actin-bundling domain revealing a ...[more]