1SYQ

Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin binding site 1, residues 607-636

Summary for 1SYQ

• Entry DOI: 10.2210/pdb1syq/pdb
• Descriptor: vinculin isoform VCL, Talin 1 (3 entities in total)
• Functional Keywords: cytoskeleton, vinculin, talin, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton: P18206; Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q9Y490
• Total number of polymer chains: 2
• Total formula weight: 32188.07

Authors

Izard, T.,Vonrhein, C. (deposition date: 2004-04-01, release date: 2004-07-20, Last modification date: 2024-02-14)

Primary citation

Izard, T.,Vonrhein, C.
Structural basis for amplifying vinculin activation by talin
J.Biol.Chem., 279:27667-27678, 2004

PubMed Abstract: Talin interactions with vinculin are essential for focal adhesions. Curiously, talin contains three noncontiguous vinculin binding sites (VBS) that can bind individually to the vinculin head (Vh) domain. Here we report the crystal structure of the human Vh.VBS1 complex, a validated model of the Vh.VBS2 structure, and biochemical studies that demonstrate that all of talin VBSs activate vinculin by provoking helical bundle conversion of the Vh domain, which displaces the vinculin tail (Vt) domain. Thus, helical bundle conversion is a structurally conserved response in talin-vinculin interactions. Furthermore, talin VBSs bind to Vh in a mutually exclusive manner but do differ in their affinity for Vh and in their ability to displace Vt, suggesting that the strengths of these interactions could lead to differences in signaling outcome. These findings support a model in which talin binds to and activates multiple vinculin molecules to provoke rapid reorganization of the actin cytoskeleton.

PubMed: 15070891
DOI: 10.1074/jbc.M403076200

Experimental method

X-RAY DIFFRACTION (2.42 Å)