3SR9

Crystal structure of mouse PTPsigma

3SR9 の概要

• エントリーDOI: 10.2210/pdb3sr9/pdb
• 分子名称: Receptor-type tyrosine-protein phosphatase S (2 entities in total)
• 機能のキーワード: tyrosine phosphatase, hydrolase
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Membrane; Single-pass type I membrane protein (Potential): B0V2N1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67207.09

構造登録者

Wang, J.,Hou, L.,Li, J.,Ding, J. (登録日: 2011-07-07, 公開日: 2012-05-30, 最終更新日: 2023-11-01)

主引用文献

Hou, L.,Wang, J.,Zhou, Y.,Li, J.,Zang, Y.,Li, J.
Structural insights into the homology and differences between mouse protein tyrosine phosphatase-sigma and human protein tyrosine phosphatase-sigma
Acta Biochim.Biophys.Sin., 43:977-988, 2011

PubMed Abstract: Protein tyrosine phosphatases PTP-sigma (PTPσ) plays an important role in the development of the nervous system and nerve regeneration. Although cumulative studies about the function of PTPσ have been reported, yet limited data have been reported about the crystal structure and in vitro activity of mouse PTPσ. Here we report the crystal structure of mouse PTPσ tandem phosphatase domains at 2.4 Å resolution. Then we compared the crystal structure of mouse PTPσ with human PTPσ and found that they are very similar, superimposing with a root mean square deviation of 0.45 Å for 517 equivalent Cα atoms. But some residues in mouse PTPσ form loops while corresponding residues in human PTPσ form β-sheets or α-helices. Furthermore, we also compared in vitro activities of mouse PTPσ with human PTPσ and found that mouse PTPσ has 25-fold higher specific activity than human PTPσ does toward O-methyl fluorescein phosphate (OMFP) as the substrate. However, there is no significant activity difference between the mouse and the human enzyme detected with p-nitrophenylphosphate (pNPP) as the substrate. Mouse PTPσ and human PTPσ have different substrate specificities toward OMFP and pNPP as substrates. This work gives clues for further study of PTPσ.

PubMed: 22027896
DOI: 10.1093/abbs/gmr095

実験手法

X-RAY DIFFRACTION (2.4 Å)