2X0C

Crystal Structure of the R7R8 domains of Talin

2X0C の概要

• エントリーDOI: 10.2210/pdb2x0c/pdb
• 関連するPDBエントリー: 1SJ7 1SJ8 1T01 1U89 1Y19 1ZW3 2B0H 2G35
• 分子名称: TALIN-1 (2 entities in total)
• 機能のキーワード: cytoskeleton, cell membrane, actin, synemin, integrin, vinculin, cell adhesion, cell projection
• 由来する生物種: MUS MUSCULUS (MOUSE)
• 細胞内の位置: Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P26039
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32574.72

構造登録者

Gingras, A.R.,Goult, B.T.,Bate, N.,Barsukov, I.L.,Emsley, J.,Critchely, D.R. (登録日: 2009-12-08, 公開日: 2010-07-07, 最終更新日: 2024-06-19)

主引用文献

Gingras, A.R.,Bate, N.,Goult, B.T.,Patel, B.,Kopp, P.M.,Emsley, J.,Barsukov, I.L.,Roberts, G.C.K.,Critchley, D.R.
Central Region of Talin Has a Unique Fold that Binds Vinculin and Actin.
J.Biol.Chem., 285:29577-, 2010

PubMed Abstract: Talin is an adaptor protein that couples integrins to F-actin. Structural studies show that the N-terminal talin head contains an atypical FERM domain, whereas the N- and C-terminal parts of the talin rod include a series of α-helical bundles. However, determining the structure of the central part of the rod has proved problematic. Residues 1359-1659 are homologous to the MESDc1 gene product, and we therefore expressed this region of talin in Escherichia coli. The crystal structure shows a unique fold comprised of a 5- and 4-helix bundle. The 5-helix bundle is composed of nonsequential helices due to insertion of the 4-helix bundle into the loop at the C terminus of helix α3. The linker connecting the bundles forms a two-stranded anti-parallel β-sheet likely limiting the relative movement of the two bundles. Because the 5-helix bundle contains the N and C termini of this module, we propose that it is linked by short loops to adjacent bundles, whereas the 4-helix bundle protrudes from the rod. This suggests the 4-helix bundle has a unique role, and its pI (7.8) is higher than other rod domains. Both helical bundles contain vinculin-binding sites but that in the isolated 5-helix bundle is cryptic, whereas that in the isolated 4-helix bundle is constitutively active. In contrast, both bundles are required for actin binding. Finally, we show that the MESDc1 protein, which is predicted to have a similar fold, is a novel actin-binding protein.

PubMed: 20610383
DOI: 10.1074/JBC.M109.095455

実験手法

X-RAY DIFFRACTION (2 Å)