2KBB

Solution Structure of the R9 Domain of Talin

2KBB の概要

• エントリーDOI: 10.2210/pdb2kbb/pdb
• NMR情報: BMRB: 15457
• 分子名称: Talin-1 (1 entity in total)
• 機能のキーワード: talin, rod, bundle, integrin, f3, cytoskeleton, autoinhibition, structural protein, cell membrane, cell projection, cytoplasm, membrane, phosphoprotein
• 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: 18247.41

構造登録者

Goult, B.T.,Gingras, A.R.,Bate, N.,Critchley, D.R.,Barsukov, I.L. (登録日: 2008-11-24, 公開日: 2009-03-17, 最終更新日: 2024-05-22)

主引用文献

Goult, B.T.,Bate, N.,Anthis, N.J.,Wegener, K.L.,Gingras, A.R.,Patel, B.,Barsukov, I.L.,Campbell, I.D.,Roberts, G.C.,Critchley, D.R.
The structure of an interdomain complex that regulates talin activity.
J.Biol.Chem., 284:15097-15106, 2009

PubMed Abstract: Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. It exists in both globular and extended conformations, and an intramolecular interaction between the N-terminal F3 FERM subdomain and the C-terminal part of the talin rod contributes to an autoinhibited form of the molecule. Here, we report the solution structure of the primary F3 binding domain within the C-terminal region of the talin rod and use intermolecular nuclear Overhauser effects to determine the structure of the complex. The rod domain (residues 1655-1822) is an amphipathic five-helix bundle; Tyr-377 of F3 docks into a hydrophobic pocket at one end of the bundle, whereas a basic loop in F3 (residues 316-326) interacts with a cluster of acidic residues in the middle of helix 4. Mutation of Glu-1770 abolishes binding. The rod domain competes with beta3-integrin tails for binding to F3, and the structure of the complex suggests that the rod is also likely to sterically inhibit binding of the FERM domain to the membrane.

PubMed: 19297334
DOI: 10.1074/jbc.M900078200

実験手法

SOLUTION NMR