PDBsum entry 3pdz

Hydrolase

PDB id: 3pdz

Contents

Protein chain

96 a.a. *

* Residue conservation analysis

PDB id:

3pdz

Name:

Hydrolase

Title:

Solution structure of the pdz2 domain from human phosphatase hptp1e

Structure:

Protein (tyrosine phosphatase (ptp-bas, type 1)). Chain: a. Fragment: pdz2 domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

30 models

Authors:

G.Kozlov,K.Gehring,I.Ekiel

Key ref:

G.Kozlov et al. (2000). Solution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptor. Biochemistry, 39, 2572-2580. PubMed id: 10704206 DOI: 10.1021/bi991913c

Date:

10-May-99 Release date: 17-Mar-00

Protein chain

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

Seq: 2485 a.a.

Struc: 96 a.a.

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: 10.1021/bi991913c

Biochemistry 39:2572-2580 (2000)

PubMed id: 10704206

Solution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptor.

G.Kozlov, K.Gehring, I.Ekiel.

ABSTRACT

The solution structure of the second PDZ domain (PDZ2) from human phosphatase hPTP1E has been determined using 2D and 3D heteronuclear NMR experiments. The binding of peptides derived from the C-terminus of the Fas receptor to PDZ2 was studied via changes in backbone peptide and protein resonances. The structure is based on a total of 1387 nonredundant experimental NMR restraints including 1261 interproton distance restraints, 45 backbone hydrogen bonds, and 81 torsion angle restraints. Analysis of 30 lowest-energy structures resulted in rmsd values of 0.41 +/- 0.09 A for backbone atoms (N, Calpha, C') and 1.08 +/- 0.10 A for all heavy atoms, excluding the disordered N- and C-termini. The hPTP1E PDZ2 structure is similar to known PDZ domain structures but contains two unique structural features. In the peptide binding domain, the first glycine of the GLGF motif is replaced by a serine. This serine appears to replace a bound water observed in PDZ crystal structures that hydrogen bonds to the bound peptide's C-terminus. The hPTP1E PDZ2 structure also contains an unusually large loop following strand beta2 and proximal to the peptide binding site. This well-ordered loop folds back against the PDZ domain and contains several residues that undergo large amide chemical shift changes upon peptide binding. Direct observation of peptide resonances demonstrates that as many as six Fas peptide residues interact with the PDZ2 domain.