Crystal Structure of Human Filamin C Domain 23 and Small Angle Scattering Model for Filamin C 23-24 Dimer.
From: International School for Advanced Studies, 34000 Trieste, Italy.
Journal of molecular biology
- Publish Date: May 2007
- ISSN: 0022-2836
- Volume: 368
- Issue: 4
- Pages: 1011-23
- Medium: Print
- Language: English
- Citation (JAMA): Sjekloća Ljiljana, Pudas Regina, Sjöblom Björn, et al. Crystal Structure of Human Filamin C Domain 23 and Small Angle Scattering Model for Filamin C 23-24 Dimer.. J. Mol. Biol. May 2007;368:1011-23
Abstract
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.
Mesh Headings (Keywords): Binding Sites, Contractile Proteins, Crystallography, X-Ray, Dimerization, Humans, Microfilament Proteins, Models, Molecular, Nickel, Protein Folding, Protein Structure, Tertiary, Scattering, Small Angle, Ultracentrifugation
Check for Full Text / PubMed Unique Identifier (PMID): 17379241
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