1K40

crystal structure of the FAT domain of focal adhesion kinase

Summary for 1K40

• Entry DOI: 10.2210/pdb1k40/pdb
• NMR Information: BMRB: 5677
• Descriptor: adhesion kinase (2 entities in total)
• Functional Keywords: helix bundle, transferase
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell junction, focal adhesion: P34152
• Total number of polymer chains: 1
• Total formula weight: 14006.39

Authors

Hayashi, I.,Vuori, K.,Liddington, R.C. (deposition date: 2001-10-04, release date: 2002-02-06, Last modification date: 2024-02-07)

Primary citation

Hayashi, I.,Vuori, K.,Liddington, R.C.
The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin
Nat.Struct.Biol., 9:101-106, 2002

PubMed Abstract: Focal adhesion kinase (FAK) is a tyrosine kinase found in focal adhesions, intracellular signaling 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. We have determined the crystal structure of FAT and show that it forms a four-helix bundle that resembles those found in two other proteins involved in cell adhesion, alpha-catenin and vinculin. 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. We show by mutagenesis that paxillin binding involves two hydrophobic patches on opposite faces of the bundle and propose a model in which two LD motifs of paxillin adopt amphipathic helices that augment the hydrophobic core of FAT, creating a six-helix bundle.

PubMed: 11799401
DOI: 10.1038/nsb755

Experimental method

X-RAY DIFFRACTION (2.25 Å)