6533b82cfe1ef96bd128f628

RESEARCH PRODUCT

Crystal Structure of Human Filamin C Domain 23 and Small Angle Scattering Model for Filamin C 23–24 Dimer

Ljiljana SjekloćaJari YlänneJari YlänneDmitri I. SvergunDmitri I. SvergunPetr V. KonarevPeter V. KonarevVladimir RybinRegina PudasBjörn SjöblomKristina Djinović CarugoOliviero CarugoTiila-riikka Kiema

subject

Models MolecularProtein FoldingFilaminsDimermacromolecular substancesCrystal structureCrystallography X-RayFilaminSarcomereAnalytical Ultracentrifugationchemistry.chemical_compoundContractile ProteinsNickelStructural BiologyScattering Small AngleHumansMolecular BiologyBinding SitesSmall-angle X-ray scatteringScatteringMicrofilament ProteinsProtein Structure TertiaryCrystallographychemistrySmall-angle scatteringDimerizationUltracentrifugation

description

Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ultracentrifugation experiments on the constructs containing carboxy-terminal domains of the protein (domains 23-24 and 19-21). The crystal structure of domain 23 of filamin C showed that the protein adopts the expected immunoglobulin (Ig)-like fold. Small-angle X-ray scattering experiments performed on filamin C tandem Ig-like domains 23 and 24 reveal a dimer that is formed by domain 24 and that domain 23 has little interactions with itself or with domain 24, while the analytical ultracentrifugation experiments showed that the filamin C domains 19-21 form elongated monomers in diluted solutions.

yearjournalcountryeditionlanguage
2007-05-01Journal of Molecular Biology
https://doi.org/10.1016/j.jmb.2007.02.018