STRUCTURE OF VINCULIN

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Vinculin is a 1066-amino-acid cytosolic protein that is a central player in the assembly of focal adhesions and associated signal transduction pathways. We recently determined the structure of the vinculin tail domain and have formulated a hypothesis of PIP2-mediated activation of the full-length molecule. We will now test this hypothesis by determining the crystal structure of the full-length vinculin to the limits of diffraction, using conventional heavy atom derivatives. Crystals contain a single molecule in the asymmetric unit, and diffract X-rays to 3.2 ¿¿resolution.