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

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 (domai...

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Bibliographic Details
Published in:Journal of molecular biology 2007-05, Vol.368 (4), p.1011-1023
Main Authors: Sjekloća, Ljiljana, Pudas, Regina, Sjöblom, Björn, Konarev, Peter, Carugo, Oliviero, Rybin, Vladimir, Kiema, Tiila-Riikka, Svergun, Dmitri, Ylänne, Jari, Carugo, Kristina Djinović
Format: Article
Language:English
Subjects:
Binding Sites
Contractile Proteins - chemistry
Crystallography, X-Ray
Dimerization
F-actin based cytoskeleton
filamin C dimer architecture
Filamins
Humans
Ig-like domain
macromolecular crystallography
Microfilament Proteins - chemistry
Models, Molecular
Nickel - chemistry
Protein Folding
Protein Structure, Tertiary
Scattering, Small Angle
small-angle X-ray scattering
Ultracentrifugation
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Summary: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.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2007.02.018