4B7L

Crystal Structure of Human Filamin B Actin Binding Domain with 1st Filamin Repeat

4B7L の概要

• エントリーDOI: 10.2210/pdb4b7l/pdb
• 関連するPDBエントリー: 2DI8 2DI9 2DIA 2DIB 2DIC 2DJ4 2WA5 2WA6 2WA7
• 分子名称: FILAMIN-B (2 entities in total)
• 機能のキーワード: structural protein, fr 1 filamin hinge abd-1
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Isoform 1: Cytoplasm, cell cortex. Isoform 2: Cytoplasm, cytoskeleton. Isoform 3: Cytoplasm, cytoskeleton. Isoform 6: Cytoplasm, cytoskeleton: O75369
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78571.66

構造登録者

Sawyer, G.M.,Sutherland-Smith, A.J. (登録日: 2012-08-20, 公開日: 2012-10-10, 最終更新日: 2023-12-20)

主引用文献

Sawyer, G.M.,Sutherland-Smith, A.J.
Crystal Structure of the Filamin N-Terminal Region Reveals a Hinge between the Actin Binding and First Repeat Domains
J.Mol.Biol., 424:240-, 2012

PubMed Abstract: The filamin proteins cross-link F-actin and interact with protein partners to integrate both extracellular and intracellular signalling events with the cytoskeleton and to provide mechanoprotection and sensing to cells. The filamins are large, flexible, multi-domain homodimers with the interactions between domains important for protein function. The crystal structure of the N-terminal region of filamin B, containing the actin binding domain (ABD) and the first filamin repeat (FR1) domain, reveals an extended two-domain conformation with no interaction between the ABD and FR1 other than the connecting linker region. The two FLNB347 structures in the crystallographic asymmetric unit exhibit differing relative domain orientations providing the first high-resolution structural characterisation of a filamin inter-domain conformational change. The structure reveals a new hinge in the linker region between ABD and FR1 that is ideally positioned to orient the ABD for actin binding and adds to the previously described hinge regions, hinge 1 (between repeats 15 and 16) and hinge 2 (repeats 23 and 24), providing an additional mechanism by which filamin can exhibit inter-domain flexibility. The extended structure, with the absence of interactions between the domains, implies that any conformational rearrangements required for actin binding by the ABD, as observed for homologous proteins, can freely occur without being influenced by FR1. The ABD retains its previously observed compact conformation. FR1 exhibits a filamin immunoglobulin-like domain fold with a closed C-D β-strand groove, in contrast to filamin repeats that bind protein partners with this region of the domain surface.

PubMed: 23036857
DOI: 10.1016/J.JMB.2012.09.016

実験手法

X-RAY DIFFRACTION (2.05 Å)