4BPC

Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic Acid Form

4BPC の概要

• エントリーDOI: 10.2210/pdb4bpc/pdb
• 分子名称: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE S (2 entities in total)
• 機能のキーワード: hydrolase, proteoglycan, redox regulation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 66932.55

構造登録者

Jeon, T.J.,Chien, P.N.,Chun, H.J.,Ryu, S.E. (登録日: 2013-05-24, 公開日: 2013-07-17, 最終更新日: 2024-10-16)

主引用文献

Jeon, T.J.,Chien, P.N.,Chun, H.J.,Ryu, S.E.
Structure of the Catalytic Domain of Protein Tyrosine Phosphatase Sigma in the Sulfenic Acid Form
Mol.Cells, 36:55-, 2013

PubMed Abstract: Protein tyrosine phosphatase sigma (PTPσ) plays a vital role in neural development. The extracellular domain of PTPσ binds to various proteoglycans, which control the activity of 2 intracellular PTP domains (D1 and D2). To understand the regulatory mechanism of PTPσ, we carried out structural and biochemical analyses of PTPσ D1D2. In the crystal structure analysis of a mutant form of D1D2 of PTPσ, we unexpectedly found that the catalytic cysteine of D1 is oxidized to cysteine sulfenic acid, while that of D2 remained in its reduced form, suggesting that D1 is more sensitive to oxidation than D2. This finding contrasts previous observations on PTPα. The cysteine sulfenic acid of D1 was further confirmed by immunoblot and mass spectrometric analyses. The stabilization of the cysteine sulfenic acid in the active site of PTP suggests that the formation of cysteine sulfenic acid may function as a stable intermediate during the redox-regulation of PTPs.

PubMed: 23820885
DOI: 10.1007/S10059-013-0033-X

実験手法

X-RAY DIFFRACTION (2.1 Å)