2QDQ

Crystal structure of the talin dimerisation domain

2QDQ の概要

• エントリーDOI: 10.2210/pdb2qdq/pdb
• 分子名称: Talin-1 (2 entities in total)
• 機能のキーワード: talin, dimerisation domain, c-terminal actin binding site, abs3, latch domain, structural protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cell projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side : P26039
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 11695.45

構造登録者

Gingras, A.R.,Putz, N.S.M.,Bate, N.,Barsukov, I.L.,Critchley, D.R.C. (登録日: 2007-06-21, 公開日: 2008-01-29, 最終更新日: 2024-02-21)

主引用文献

Gingras, A.R.,Bate, N.,Goult, B.T.,Hazelwood, L.,Canestrelli, I.,Grossmann, J.G.,Liu, H.,Putz, N.S.,Roberts, G.C.,Volkmann, N.,Hanein, D.,Barsukov, I.L.,Critchley, D.R.
The structure of the C-terminal actin-binding domain of talin.
Embo J., 27:458-469, 2008

PubMed Abstract: Talin is a large dimeric protein that couples integrins to cytoskeletal actin. Here, we report the structure of the C-terminal actin-binding domain of talin, the core of which is a five-helix bundle linked to a C-terminal helix responsible for dimerisation. The NMR structure of the bundle reveals a conserved surface-exposed hydrophobic patch surrounded by positively charged groups. We have mapped the actin-binding site to this surface and shown that helix 1 on the opposite side of the bundle negatively regulates actin binding. The crystal structure of the dimerisation helix reveals an antiparallel coiled-coil with conserved residues clustered on the solvent-exposed face. Mutagenesis shows that dimerisation is essential for filamentous actin (F-actin) binding and indicates that the dimerisation helix itself contributes to binding. We have used these structures together with small angle X-ray scattering to derive a model of the entire domain. Electron microscopy provides direct evidence for binding of the dimer to F-actin and indicates that it binds to three monomers along the long-pitch helix of the actin filament.

PubMed: 18157087
DOI: 10.1038/sj.emboj.7601965

実験手法

X-RAY DIFFRACTION (2.2 Å)