1PTU

CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH PHOSPHOTYROSINE-CONTAINING HEXA-PEPTIDE (DADEPYL-NH2)

Summary for 1PTU

• Entry DOI: 10.2210/pdb1ptu/pdb
• Descriptor: PROTEIN TYROSINE PHOSPHATASE 1B, PHOSPHOTYROSINE-CONTAINING HEXA-PEPTIDE (3 entities in total)
• Functional Keywords: hydrolase, acetylation, phosphorylation, complex (hydrolase-peptide) complex, complex (hydrolase/peptide)
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side: P18031
• Total number of polymer chains: 2
• Total formula weight: 38166.30

Authors

Barford, D.,Jia, Z. (deposition date: 1995-04-21, release date: 1996-08-01, Last modification date: 2024-10-30)

Primary citation

Jia, Z.,Barford, D.,Flint, A.J.,Tonks, N.K.
Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B.
Science, 268:1754-1758, 1995

PubMed Abstract: The crystal structures of a cysteine-215-->serine mutant of protein tyrosine phosphatase 1B complexed with high-affinity peptide substrates corresponding to an autophosphorylation site of the epidermal growth factor receptor were determined. Peptide binding to the protein phosphatase was accompanied by a conformational change of a surface loop that created a phosphotyrosine recognition pocket and induced a catalytically competent form of the enzyme. The phosphotyrosine side chain is buried within the period and anchors the peptide substrate to its binding site. Hydrogen bonds between peptide main-chain atoms and the protein contribute to binding affinity, and specific interactions of acidic residues of the peptide with basic residues on the surface of the enzyme confer sequence specificity.

PubMed: 7540771

Experimental method

X-RAY DIFFRACTION (2.6 Å)