6533b85dfe1ef96bd12be978
RESEARCH PRODUCT
Novel structural insights into F-actin-binding and novel functions of calponin homology domains.
Jari YlänneKristina Djinović CarugoKristina Djinović-carugoBjörn Sjöblomsubject
biologyTandemChemistryDimerCalponinCalcium-Binding ProteinsMicrofilament ProteinsF-actin bindingmacromolecular substancesMicrotubulesActinschemistry.chemical_compoundCrystallographyActin CytoskeletonMicroscopy ElectronStructural BiologyStructural Homology Proteinbiology.proteinProtein Interaction Domains and MotifsPaxillinMolecular BiologyActinPaxillinMacromoleculeProtein Bindingdescription
Tandem calponin homology (CH) domains are well-known actin filaments (F-actin) binding motifs. There has been a continuous debate about the details of CH domain-actin interaction, mainly because atomic level structures of F-actin are not available. A recent electron microscopy study has considerably advanced our structural understanding of CH domain:F-actin complex. On the contrary, it has recently also been shown that CH domains can bind other macromolecular systems: two CH domains from separate polypeptides Ncd80, Nuf2 can form a microtubule-binding site, as well as tandem CH domains in the EB1 dimer, while the single C-terminal CH domain of alpha-parvin has been observed to bind to a alpha-helical leucin-aspartate rich motif from paxillin.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2008-12-01 |