PDBsum entry 1pv3

Transferase

PDB id: 1pv3

Contents

Protein chain

146 a.a. *

* Residue conservation analysis

PDB id:

1pv3

Name:

Transferase

Title:

Nmr solution structure of the avian fat-domain of focal adhesion kinase

Structure:

Focal adhesion kinase 1. Chain: a. Fragment: focal adhesion targeting (fat) domain. Synonym: fadk 1, pp125fak. Engineered: yes

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Gene: fak1 or fak. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

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

Key ref:

K.C.Prutzman et al. (2004). The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation. Structure, 12, 881-891. PubMed id: 15130480 DOI: 10.1016/j.str.2004.02.028

Date:

26-Jun-03 Release date: 25-May-04

Protein chain

Q00944  (FAK1_CHICK) -  Focal adhesion kinase 1 from Gallus gallus

Seq: 1053 a.a.

Struc: 146 a.a.*

* PDB and UniProt seqs differ at 12 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.7.10.2 - non-specific protein-tyrosine kinase.
• Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/j.str.2004.02.028

Structure 12:881-891 (2004)

PubMed id: 15130480

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

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

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.

Selected figure(s)

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).

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 881-891) copyright 2004.

Figure was selected by an automated process.