1PV3

NMR Solution Structure of the Avian FAT-domain of Focal Adhesion Kinase

Summary for 1PV3

• Entry DOI: 10.2210/pdb1pv3/pdb
• Descriptor: Focal adhesion kinase 1 (1 entity in total)
• Functional Keywords: focal adhesion kinase, helix bundle, fat-domain, transferase
• Biological source: Gallus gallus (chicken)
• Cellular location: Cell junction, focal adhesion : Q00944
• Total number of polymer chains: 1
• Total formula weight: 15897.43

Authors

Prutzman, K.C.,Gao, G.,King, M.L.,Iyer, V.V.,Mueller, G.A.,Schaller, M.D.,Campbell, S.L. (deposition date: 2003-06-26, release date: 2004-05-25, Last modification date: 2024-05-01)

Primary citation

Prutzman, K.C.,Gao, G.,King, M.L.,Iyer, V.V.,Mueller, G.A.,Schaller, M.D.,Campbell, S.L.
The Focal Adhesion Targeting Domain of Focal Adhesion Kinase Contains a Hinge Region that Modulates Tyrosine 926 Phosphorylation.
STRUCTURE, 12:881-891, 2004

PubMed Abstract: The focal adhesion targeting (FAT) domain of focal adhesion kinase (FAK) is critical for recruitment of FAK to focal adhesions and contains tyrosine 926, which, when phosphorylated, binds the SH2 domain of Grb2. Structural studies have shown that the FAT domain is a four-helix bundle that exists as a monomer and a dimer due to domain swapping of helix 1. Here, we report the NMR solution structure of the avian FAT domain, which is similar in overall structure to the X-ray crystal structures of monomeric forms of the FAT domain, except that loop 1 is longer and less structured in solution. Residues in this region undergo temperature-dependent exchange broadening and sample aberrant phi and psi angles, which suggests that this region samples multiple conformations. We have also identified a mutant that dimerizes approximately 8 fold more than WT FAT domain and exhibits increased phosphorylation of tyrosine 926 both in vitro and in vivo.

PubMed: 15130480
DOI: 10.1016/j.str.2004.02.028

Experimental method

SOLUTION NMR