2GWO

crystal structure of TMDP

2GWO の概要

• エントリーDOI: 10.2210/pdb2gwo/pdb
• 分子名称: Dual specificity protein phosphatase 13 (2 entities in total)
• 機能のキーワード: alpha/beta, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 88698.38

構造登録者

Kim, S.J.,Ryu, S.E.,Kim, J.H. (登録日: 2006-05-05, 公開日: 2007-03-20, 最終更新日: 2024-03-13)

主引用文献

Kim, S.J.,Jeong, D.G.,Yoon, T.S.,Son, J.H.,Cho, S.K.,Ryu, S.E.,Kim, J.H.
Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity
Proteins, 66:239-245, 2007

PubMed Abstract: The testis- and skeletal-muscle-specific dual-specificity phosphatase (TMDP) is a member of the dual-specificity phosphatase (DSP) subgroup of protein tyrosine phosphatases. TMDP has similar activities toward both tyrosine and threonine phosphorylated substrates, and is supposed to be involved in spermatogenesis. Here, we report the crystal structure of human TMDP at a resolution of 2.4 A. In spite of high sequence similarity with other DSPs, the crystal structure of TMDP shows distinct structural motifs and surface properties. In TMDP, the alpha1-beta1 loop, a substrate recognition motif is located further away from the active site loop in comparison to prototype DSP Vaccinia H1 related phophatase (VHR), which preferentially dephosphorylates tyrosine phosphorylated substrates and down-regulates MAP kinase signaling. Residues in the active site residues of TMDP are smaller in size and more hydrophobic than those of VHR. In addition, TMDP cannot be aligned with VHR in loop beta3-alpha4. These differences in the active site of TMDP result in a flat and wide pocket structure, allowing equal binding of phosphotyrosine and phosphothreonine substrates.

PubMed: 17044055
DOI: 10.1002/prot.21197

実験手法

X-RAY DIFFRACTION (2.4 Å)