1PTV

CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH PHOSPHOTYROSINE

1PTV の概要

• エントリーDOI: 10.2210/pdb1ptv/pdb
• 分子名称: PROTEIN TYROSINE PHOSPHATASE 1B, O-PHOSPHOTYROSINE (3 entities in total)
• 機能のキーワード: hydrolase, acetylation, phosphorylation, complex (hydrolase-peptide) complex, complex (hydrolase/peptide)
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side: P18031
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37610.74

構造登録者

Barford, D.,Jia, Z. (登録日: 1995-04-21, 公開日: 1996-08-01, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)