Focal adhesion targeting region | |||||||||
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crystal structure of the fat domain of focal adhesion kinase | |||||||||
Identifiers | |||||||||
Symbol | Focal_AT | ||||||||
Pfam | PF03623 | ||||||||
InterPro | IPR005189 | ||||||||
SCOP | 1ktm | ||||||||
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In molecula biology, the focal adhesion targeting region is a conserved domain found on focal adhesion kinases. Focal adhesion kinases (FAK) are tyrosine kinases found in focal adhesions, intracellular signalling complexes that are formed following engagement of the extracellular matrix by integrins. The C-terminal focal adhesion targeting (FAT) region is necessary and sufficient for localizing FAK to focal adhesions. The crystal structure of FAT shows it forms a four-helix bundle that resembles those found in two other proteins involved in cell adhesion, alpha-catenin and vinculin.[1] The binding of FAT to the focal adhesion protein, paxillin, requires the integrity of the helical bundle, whereas binding to another focal adhesion protein, talin, does not.
Eukaryotic Linear Motif resource motif class LIG_FAT_LD_1
This article incorporates text from the public domain Pfam and InterPro IPR005189