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PDBsum entry 5eyz
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PDB id:
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Apoptosis
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Title:
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Crystal structure of the ptpn4 pdz domain complexed with the tailored peptide cyto8-retev
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Structure:
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Tyrosine-protein phosphatase non-receptor type 4. Chain: a, b, c, d. Fragment: pdz domain, residues 499-604. Synonym: protein-tyrosine phosphatase meg1,ptpase-meg1. Engineered: yes. Cyto8-retev. Chain: e, f, g, h. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ptpn4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: star. Synthetic: yes. Synthetic construct.
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Resolution:
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2.09Å
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R-factor:
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0.230
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R-free:
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0.240
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Authors:
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P.Maisonneuve,M.C.Vaney,B.Babault,C.Caillet-Saguy,M.Lafon, M.Delepierre,F.Cordier,N.Wolff
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Key ref:
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P.Maisonneuve
et al.
(2016).
Molecular Basis of the Interaction of the Human Protein Tyrosine Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein Kinase p38γ.
J Biol Chem,
291,
16699-16708.
PubMed id:
DOI:
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Date:
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26-Nov-15
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Release date:
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08-Jun-16
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PROCHECK
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Headers
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References
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P29074
(PTN4_HUMAN) -
Tyrosine-protein phosphatase non-receptor type 4 from Homo sapiens
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Seq:
Struc:
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926 a.a.
93 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.1.3.48
- protein-tyrosine-phosphatase.
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Reaction:
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O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate
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O-phospho-L-tyrosyl-[protein]
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+
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H2O
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=
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L-tyrosyl-[protein]
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+
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phosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Biol Chem
291:16699-16708
(2016)
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PubMed id:
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Molecular Basis of the Interaction of the Human Protein Tyrosine Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein Kinase p38γ.
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P.Maisonneuve,
C.Caillet-Saguy,
M.C.Vaney,
E.Bibi-Zainab,
K.Sawyer,
B.Raynal,
A.Haouz,
M.Delepierre,
M.Lafon,
F.Cordier,
N.Wolff.
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ABSTRACT
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The human protein tyrosine phosphatase non-receptor type 4 (PTPN4) prevents cell
death induction in neuroblastoma and glioblastoma cell lines in a PDZ·PDZ
binding motifs-dependent manner, but the cellular partners of PTPN4 involved in
cell protection are unknown. Here, we described the mitogen-activated protein
kinase p38γ as a cellular partner of PTPN4. The main contribution to the
p38γ·PTPN4 complex formation is the tight interaction between the C terminus
of p38γ and the PDZ domain of PTPN4. We solved the crystal structure of the PDZ
domain of PTPN4 bound to the p38γ C terminus. We identified the molecular basis
of recognition of the C-terminal sequence of p38γ that displays the highest
affinity among all endogenous partners of PTPN4. We showed that the p38γ C
terminus is also an efficient inducer of cell death after its intracellular
delivery. In addition to recruiting the kinase, the binding of the C-terminal
sequence of p38γ to PTPN4 abolishes the catalytic autoinhibition of PTPN4 and
thus activates the phosphatase, which can efficiently dephosphorylate the
activation loop of p38γ. We presume that the p38γ·PTPN4 interaction promotes
cellular signaling, preventing cell death induction.
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