PDBsum entry 1gl5

Transferase

PDB id: 1gl5

Contents

Protein chain

67 a.a. *

* Residue conservation analysis

PDB id:

1gl5

Name:

Transferase

Title:

Nmr structure of the sh3 domain from the tec protein tyrosine kinase

Structure:

Tyrosine-protein kinase tec. Chain: a. Fragment: sh3 domain (181-245). Engineered: yes. Other_details: n-terminal gly-ser from glutathione s-transferase fusion partner

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: gst-fusion

NMR struc:

20 models

Authors:

T.D.Mulhern,S.E.Pursglove,G.W.Booker

Key ref:

S.E.Pursglove et al. (2002). The solution structure and intramolecular associations of the Tec kinase SRC homology 3 domain. J Biol Chem, 277, 755-762. PubMed id: 11684687

Date:

28-Aug-01 Release date: 28-Nov-01

Protein chain

P24604  (TEC_MOUSE) -  Tyrosine-protein kinase Tec from Mus musculus

Seq: 630 a.a.

Struc: 67 a.a.*

* PDB and UniProt seqs differ at 3 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

J Biol Chem 277:755-762 (2002)

PubMed id: 11684687

The solution structure and intramolecular associations of the Tec kinase SRC homology 3 domain.

S.E.Pursglove, T.D.Mulhern, J.P.Mackay, M.G.Hinds, G.W.Booker.

ABSTRACT

Tec is the prototypic member of a family of intracellular tyrosine kinases that includes Txk, Bmx, Itk, and Btk. Tec family kinases share similarities in domain structure with Src family kinases, but one of the features that differentiates them is a proline-rich region (PRR) preceding their Src homology (SH) 3 domain. Evidence that the PRR of Itk can bind in an intramolecular fashion to its SH3 domain and the lack of a regulatory tyrosine in the C terminus indicates that Tec kinases must be regulated by a different set of intramolecular interactions to the Src kinases. We have determined the solution structure of the Tec SH3 domain and have investigated interactions with its PRR, which contains two SH3-binding sites. We demonstrate that in vitro, the Tec PRR can bind in an intramolecular fashion to the SH3. However, the affinity is lower than that for dimerization via reciprocal PRR-SH3 association. Using site-directed mutagenesis we show that both sites can bind the Tec SH3 domain; site 1 (155KTLPPAP161) binds intramolecularly, while site 2 (165KRRPPPPIPP174) cannot and binds in an intermolecular fashion. These distinct roles for the SH3 binding sites in Tec family kinases could be important for protein targeting and enzyme activation.