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TitleCrystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer.
Journal, issue, pagesJ Mol Biol, Vol. 368, Issue 4, Page 1011-1023, Year 2007
Publish dateMay 11, 2007
AuthorsLjiljana Sjekloća / Regina Pudas / Björn Sjöblom / Peter Konarev / Oliviero Carugo / Vladimir Rybin / Tiila-Riikka Kiema / Dmitri Svergun / Jari Ylänne / Kristina Djinović Carugo /
PubMed AbstractFilamin 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 ...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.
External linksJ Mol Biol / PubMed:17379241
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.05 Å
Structure data

SASDAC4:
FilaminC 23-24 (Filamin C 23-24)
Method: SAXS/SANS

PDB-2nqc:
Crystal structure of ig-like domain 23 from human filamin C
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION

ChemComp-IMD:
IMIDAZOLE

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • Escherichia coli (E. coli)
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / FILAMIN / IMMUNOGLOBULIN / METAL BINDING

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