3LK2

Crystal structure of CapZ bound to the uncapping motif from CARMIL

3LK2 の概要

• エントリーDOI: 10.2210/pdb3lk2/pdb
• 関連するPDBエントリー: 1IZN
• 分子名称: F-actin-capping protein subunit alpha-1, F-actin-capping protein subunit beta isoforms 1 and 2, Leucine-rich repeat-containing protein 16A, ... (4 entities in total)
• 機能のキーワード: capz, carmil, actin filaments, uncapping, actin-filament regulators, protein-protein complex, actin capping, actin-binding, cytoskeleton, protein binding
• 由来する生物種: Gallus gallus (chicken); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 66238.42

構造登録者

Hernandez-Valladares, M.,Kim, T.,Kannan, B.,Tung, A.,Aguda, A.H.,Larsson, M.,Cooper, J.A.,Robinson, R.C. (登録日: 2010-01-27, 公開日: 2010-04-07, 最終更新日: 2023-11-01)

主引用文献

Hernandez-Valladares, M.,Kim, T.,Kannan, B.,Tung, A.,Aguda, A.H.,Larsson, M.,Cooper, J.A.,Robinson, R.C.
Structural characterization of a capping protein interaction motif defines a family of actin filament regulators.
Nat.Struct.Mol.Biol., 17:497-503, 2010

PubMed Abstract: Capping protein (CP) regulates actin dynamics by binding the barbed ends of actin filaments. Removal of CP may be one means to harness actin polymerization for processes such as cell movement and endocytosis. Here we structurally and biochemically investigated a CP interaction (CPI) motif present in the otherwise unrelated proteins CARMIL and CD2AP. The CPI motif wraps around the stalk of the mushroom-shaped CP at a site distant from the actin-binding interface, which lies on the top of the mushroom cap. We propose that the CPI motif may act as an allosteric modulator, restricting CP to a low-affinity, filament-binding conformation. Structure-based sequence alignments extend the CPI motif-containing family to include CIN85, CKIP-1, CapZIP and a relatively uncharacterized protein, WASHCAP (FAM21). Peptides comprising these CPI motifs are able to inhibit CP and to uncap CP-bound actin filaments.

PubMed: 20357771
DOI: 10.1038/nsmb.1792

実験手法

X-RAY DIFFRACTION (2.2 Å)