PDBsum entry 1pv3

Transferase

PDB id

1pv3

Contents

			Protein chain

					146 a.a. *

* Residue conservation analysis

References listed in PDB file

Key reference

Title

The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation.

Authors

K.C.Prutzman, G.Gao, M.L.King, V.V.Iyer, G.A.Mueller, M.D.Schaller, S.L.Campbell.

Ref.

Structure, 2004, 12, 881-891. [DOI no: 10.1016/j.str.2004.02.028]

PubMed id

15130480

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.



	Figure 1. Figure 1. Solution Structure of the Avian FAT Domain(A) Backbone atom trace of the 20 lowest energy solution structures of the avian FAT domain (residues 920-1053), with a 12 amino acid linker at the amino terminus remaining from purification.(B) The backbone trace of the avian FAT domain minus the 12 amino acid linker. The proposed hinge region (residues 941-951) is colored red.(C) Expanded view of the hinge region, which contains three prolines (P945, P947, and P948, in red).

PROCHECK

	Headers