1VHR

HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE

1VHR の概要

• エントリーDOI: 10.2210/pdb1vhr/pdb
• 分子名称: HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE VHR, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, protein dual-specificity phosphatase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P51452
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41074.52

構造登録者

Yuvaniyama, J.,Denu, J.M.,Dixon, J.E.,Saper, M.A. (登録日: 1996-02-20, 公開日: 1996-06-20, 最終更新日: 2024-02-14)

主引用文献

Yuvaniyama, J.,Denu, J.M.,Dixon, J.E.,Saper, M.A.
Crystal structure of the dual specificity protein phosphatase VHR.
Science, 272:1328-1331, 1996

PubMed Abstract: Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. Here, the crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), was determined at 2.1 angstrom resolution. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine. Positively charged crevices near the active site may explain the enzyme's preference for substrates with two phosphorylated residues. The VHR structure defines a conserved structural scaffold for both DSPs and PTPs. A "recognition region," connecting helix alpha1 to strand beta1, may determine differences in substrate specificity between VHR, the PTPs, and other DSPs.

PubMed: 8650541

実験手法

X-RAY DIFFRACTION (2.1 Å)