2KGX

HADDOCK structure of the talin F3 domain in complex with talin 1655-1822

Summary for 2KGX

• Entry DOI: 10.2210/pdb2kgx/pdb
• Related: 2h7d 2kbb
• Descriptor: Talin-1, MKIAA1027 protein (2 entities in total)
• Functional Keywords: talin, interdomain, f3, cytoskeleton, cell membrane, cell projection, cytoplasm, membrane, phosphoprotein, cell adhesion
• Biological source: Mus musculus (mouse); More
• Cellular location: Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P26039
• Total number of polymer chains: 2
• Total formula weight: 28737.51

Authors

Goult, B.T.,Gingras, A.R.,Bate, N.,Critchley, D.R.,Barsukov, I.L. (deposition date: 2009-03-23, release date: 2009-03-31, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR