Rhombohedral crystals of the human vinculin head domain in complex with a vinculin-binding site of talin

Authors: Rush, Christina L.; Izard, Tina

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 945-947(3)

Publisher: Blackwell Publishing

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Abstract:

Intermolecular interactions between the cytoskeletal proteins talin and vinculin are required for outside-in integrin signaling triggered by the formation of focal adhesions. Talin possesses three non-contiguous vinculin-binding sites (VBS); binding of one of these motifs, VBS3, provokes dramatic alterations in the structure of the vinculin's head (Vh) domain and this activates vinculin (Izard et al., 2004). To address the role of talin's other VBSs in vinculin activation, talin VBS1 (human residues 607-636) was crystallized in complex with the Vh (human residues 1-258) domain. Rhombohedral crystals of human Vh-VBS1 were obtained. The crystals belong to space group R32, with unit-cell parameters a = 88.7 Å, α = 105.5° and diffract to 2.4 Å on a third-generation synchrotron source. The packing density for one heterodimer in the asymmetric unit is 3.04 Å³ Da⁻¹, with a solvent content of 0.59.

Keywords: vinculin; talin

Document Type: Research article

DOI: 10.1107/S0907444904006547

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