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 (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.
Sjekloća
Ljiljana
L
International School for Advanced Studies, 34000 Trieste, Italy.
Pudas
Regina
R
Sjöblom
Björn
B
Konarev
Peter
P
Carugo
Oliviero
O
Rybin
Vladimir
V
Kiema
Tiila-Riikka
TR
Svergun
Dmitri
D
Ylänne
Jari
J
Djinović Carugo
Kristina
K
D001665:Binding Sites; D003285:Contractile Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D019281:Dimerization; D064448:Filamins; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry*; D008958:Models, Molecular; D009532:Nickel / Q000737:chemistry; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D053838:Scattering, Small Angle; D014461:Ultracentrifugation
D003285:Contractile Proteins; D064448:Filamins; D008840:Microfilament Proteins; D009532:Nickel