2K7P

Filamin A Ig-like domains 16-17

2K7P の概要

• エントリーDOI: 10.2210/pdb2k7p/pdb
• 関連するPDBエントリー: 2K7Q
• NMR情報: BMRB: 15924
• 分子名称: Filamin-A (1 entity in total)
• 機能のキーワード: filamin, ig-like, abp-280, actin binding protein, acetylation, actin-binding, cytoplasm, cytoskeleton, disease mutation, phosphoprotein, polymorphism, structural protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm, cell cortex: P21333
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20013.45

構造登録者

Heikkinen, O.K.,Kilpelainen, I.,Koskela, H.,Permi, P.,Heikkinen, S.,Ylanne, J. (登録日: 2008-08-19, 公開日: 2009-07-07, 最終更新日: 2024-05-29)

主引用文献

Heikkinen, O.K.,Ruskamo, S.,Konarev, P.V.,Svergun, D.I.,Iivanainen, T.,Heikkinen, S.M.,Permi, P.,Koskela, H.,Kilpelainen, I.,Ylanne, J.
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin
J.Biol.Chem., 284:25450-25458, 2009

PubMed Abstract: Filamins are actin filament cross-linking proteins composed of an N-terminal actin-binding domain and 24 immunoglobulin-like domains (IgFLNs). Filamins interact with numerous proteins, including the cytoplasmic domains of plasma membrane signaling and cell adhesion receptors. Thereby filamins mechanically and functionally link the cell membrane to the cytoskeleton. Most of the interactions have been mapped to the C-terminal IgFLNs 16-24. Similarly, as with the previously known compact domain pair of IgFLNa20-21, the two-domain fragments IgFLNa16-17 and IgFLNa18-19 were more compact in small angle x-ray scattering analysis than would be expected for two independent domains. Solution state NMR structures revealed that the domain packing in IgFLNa18-19 resembles the structure of IgFLNa20-21. In both domain pairs the integrin-binding site is masked, although the details of the domain-domain interaction are partly distinct. The structure of IgFLNa16-17 revealed a new domain packing mode where the adhesion receptor binding site of domain 17 is not masked. Sequence comparison suggests that similar packing of three tandem filamin domain pairs is present throughout the animal kingdom, and we propose that this packing is involved in the regulation of filamin interactions through a mechanosensor mechanism.

PubMed: 19622754
DOI: 10.1074/jbc.M109.019661

実験手法

SOLUTION NMR