Abstract
Abstract: Focal adhesion kinase (FAK) is a structurally distinctive cytoplasmic tyrosine kinase which localizes to cellular focal contacts. Sequences near the C-terrninus of FAK, termed the focal adhesion targeting (FAT) domain, are responsible for localization of FAK to focal adhesion complexes. Here, we report expression in E. coli of Cterminal fragments of human FAK containing the FAT domain as epitope-tagged fusions. Purified bacterially derived FAT domains were biologically active and their far ultraviolet circular dichroism spectra showed evidence of extensive alpha-helical secondary structure,
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