PDBsum entry 5glj

Hydrolase

PDB id: 5glj

Contents

Protein chains

96 a.a.

Metals

_CL ×4

Waters ×491

PDB id:

5glj

Name:

Hydrolase

Title:

Crystal structure of pdz1 domain of human protein tyrosine phosphatase ptp-bas

Structure:

Tyrosine-protein phosphatase non-receptor type 13. Chain: a, b, c, d. Fragment: pdz1 domain (unp residues 1086-1178). Synonym: fas-associated protein-tyrosine phosphatase 1,fap-1,ptp-bas, protein-tyrosine phosphatase 1e,hptpe1,protein-tyrosine phosphatase ptpl1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ptpn13, pnp1, ptp1e, ptpl1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.60Å R-factor: 0.172 R-free: 0.206

Authors:

S.O.Lee,B.Ku,S.W.Chi

Key ref:

S.O.Lee et al. (2016). High-resolution crystal structure of the PDZ1 domain of human protein tyrosine phosphatase PTP-Bas. Biochem Biophys Res Commun, 478, 1205-1210. PubMed id: 27544031 DOI: 10.1016/j.bbrc.2016.08.095

Date:

11-Jul-16 Release date: 23-Nov-16

Protein chains

Q12923  (PTN13_HUMAN) -  Tyrosine-protein phosphatase non-receptor type 13 from Homo sapiens

Seq: 2485 a.a.

Struc: 96 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.3.48 - protein-tyrosine-phosphatase.
• Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate

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

Key reference

DOI no: 10.1016/j.bbrc.2016.08.095

Biochem Biophys Res Commun 478:1205-1210 (2016)

PubMed id: 27544031

High-resolution crystal structure of the PDZ1 domain of human protein tyrosine phosphatase PTP-Bas.

S.O.Lee, M.K.Lee, B.Ku, K.H.Bae, S.C.Lee, H.M.Lim, S.J.Kim, S.W.Chi.

ABSTRACT

Protein tyrosine phosphatase-Basophil (PTP-Bas) is a membrane-associated protein tyrosine phosphatase with five PDZ domains and is involved in apoptosis, tumorigenesis, and insulin signaling. The interaction between PTP-Bas and tandem-PH-domain-containing protein 1/2 (TAPP1/2) plays an essential role in the regulation of insulin signaling. Despite its high sequence homology with the other PDZ domains, only the PDZ1 domain of PTP-Bas showed distinct binding specificity for TAPP1/2. Although the interaction between PTP-Bas PDZ1 and TAPP1/2 is a therapeutic target for diabetes, the structural basis for the interaction has not been elucidated. In the present study, we determined the crystal structure of the PTP-Bas PDZ1 domain at 1.6 Å resolution. In addition, we calculated the structural models of complexes of PTP-Bas PDZ1 and the C-terminal peptides of TAPP1/2 (referred to as TAPP1p/2p). Structural comparison with the PTP-Bas PDZ2/RA-GEF2 peptide complex revealed a structural basis for distinct binding specificity of PTP-Bas PDZ1 for TAPP1p/2p peptides. Our high-resolution crystal structure of PTP-Bas PDZ1 will serve as a useful template for rational structure-based design of novel anti-diabetes therapeutics.