2NQC

Crystal structure of ig-like domain 23 from human filamin C

Summary for 2NQC

• Entry DOI: 10.2210/pdb2nqc/pdb
• Descriptor: Filamin-C, NICKEL (II) ION, IMIDAZOLE, ... (5 entities in total)
• Functional Keywords: filamin, immunoglobulin, metal binding, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : Q14315
• Total number of polymer chains: 1
• Total formula weight: 14303.65

Authors

Sjekloca, L.,Pudas, R.,Sjoeblom, B.,Konarev, P.,Carugo, O.,Rybin, V.,Kiema, T.R.,Svergun, D.,Ylanne, J.,Djinovic-Carugo, K. (deposition date: 2006-10-31, release date: 2007-09-11, Last modification date: 2023-12-27)

Primary citation

Sjekloca, L.,Pudas, R.,Sjoeblom, B.,Konarev, P.,Carugo, O.,Rybin, V.,Kiema, T.R.,Svergun, D.,Ylanne, J.,Djinovic-Carugo, K.
Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer
J.Mol.Biol., 368:1011-1023, 2007

PubMed 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.

PubMed: 17379241
DOI: 10.1016/j.jmb.2007.02.018

Experimental method

X-RAY DIFFRACTION (2.05 Å)