ジャーナル: J Biol Chem / 年: 2009 タイトル: Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. 著者: Outi K Heikkinen / Salla Ruskamo / Peter V Konarev / Dmitri I Svergun / Tatu Iivanainen / Sami M Heikkinen / Perttu Permi / Harri Koskela / Ilkka Kilpeläinen / Jari Ylänne / 要旨: 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 ...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.
Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... andKollm
精密化
精密化
手法: molecular dynamics / ソフトェア番号: 1 / 詳細: implicit Born solvent model
NMR constraints
NOE constraints total: 2930 / NOE long range total count: 1467 / NOE medium range total count: 331 / Protein phi angle constraints total count: 117 / Protein psi angle constraints total count: 117
代表構造
選択基準: lowest energy
NMRアンサンブル
コンフォーマー選択の基準: structures with the lowest energy 計算したコンフォーマーの数: 200 / 登録したコンフォーマーの数: 20 / Maximum torsion angle constraint violation: 14.22 ° / Maximum upper distance constraint violation: 0.22 Å / 代表コンフォーマー: 19