PDBsum entry 4htj

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protein links
Hydrolase PDB id
Protein chain
89 a.a.
Waters ×34
PDB id:
Name: Hydrolase
Title: Crystallographic structure of the membrane-proximal ectodoma human receptor-type protein-tyrosine phosphatase phogrin at
Structure: Receptor-type tyrosine-protein phosphatase n2. Chain: a. Fragment: sequence database residues 502 - 599. Synonym: r-ptp-n2, islet cell autoantigen-related protein, icaar, phogrin. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ptprn2, kiaa0387. Expressed in: escherichia coli. Expression_system_taxid: 562
2.01Å     R-factor:   0.204     R-free:   0.238
Authors: M.E.Noguera,J.Jakoncic,E.Poskus,M.R.Ermacora
Key ref: M.E.Noguera et al. (2013). Biophysical characterization of the membrane-proximal ectodomain of the receptor-type protein-tyrosine phosphatase phogrin. Protein Pept Lett, 20, 1009-1017. PubMed id: 23016632
01-Nov-12     Release date:   28-Nov-12    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q92932  (PTPR2_HUMAN) -  Receptor-type tyrosine-protein phosphatase N2
1015 a.a.
89 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= protein tyrosine
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site


Protein Pept Lett 20:1009-1017 (2013)
PubMed id: 23016632  
Biophysical characterization of the membrane-proximal ectodomain of the receptor-type protein-tyrosine phosphatase phogrin.
M.E.Noguera, M.E.Primo, L.N.Sosa, V.A.Risso, E.Poskus, M.R.Ermácora.
The receptor-type protein-tyrosine phosphatase (RPTP) phogrin is localized at the membrane of secretory granules of pancreatic islet β-cells and, similarly to the closely related ICA512, plays a role in the regulation of insulin secretion, in ensuring proper granulogenesis and stability, and in the regulation of β-cell growth. The mature membraneproximal ectodomain of phogrin (MPE phogrin) was produced as a recombinant protein and characterized. CD, fluorescence, controlled proteolysis, size-exclusion chromatography, and multi-angle light scattering showed that it is a properlyfolded monomeric domain. Equilibrium experiments, in the presence of guanidinium chloride and thermal unfolding, suggest a two-state mechanism with a ΔG of 2.3-3.3 kcal/mol, respectively. The study establishes common features and differences of MPE phogrin and the homologous ectodomain of ICA512. A homology model of phogrin was built based in the x-ray structure of MPE ICA512. The model is a starting point for modeling the entire receptor and for testing the quaternary structure and interactions of this protein in vivo. A description of the membrane insertion mode and putative interacting surfaces of this large protein is fundamental for the understanding of its biological function.