5J8R

Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 12 - K61R mutant

5J8R の概要

• エントリーDOI: 10.2210/pdb5j8r/pdb
• 分子名称: Tyrosine-protein phosphatase non-receptor type 12 (2 entities in total)
• 機能のキーワード: cancer, tyrosine phosphorylation, hydrolase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm : Q05209
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 148185.00

構造登録者

Li, H.,Yang, F.,Xu, Y.F.,Wang, W.J.,Xiao, P.,Yu, X.,Sun, J.P. (登録日: 2016-04-08, 公開日: 2016-04-27, 最終更新日: 2023-11-08)

主引用文献

Li, H.,Yang, F.,Liu, C.,Xiao, P.,Xu, Y.F.,Liang, Z.L.,Liu, C.,Wang, H.M.,Wang, W.J.,Zheng, W.S.,Zhang, W.,Ma, X.Y.,He, D.F.,Song, X.Y.,Cui, F.A.,Xu, Z.G.,Yi, F.,Sun, J.P.,Yu, X.
Crystal structure and substrate specificity of PTPN12.
Cell Rep, 15:1-14, 2016

PubMed Abstract: PTPN12 is an important tumor suppressor that plays critical roles in various physiological processes. However, the molecular basis underlying the substrate specificity of PTPN12 remains uncertain. Here, enzymological and crystallographic studies have enabled us to identify two distinct structural features that are crucial determinants of PTPN12 substrate specificity: the pY+1 site binding pocket and specific basic charged residues along its surface loops. Key structurally plastic regions and specific residues in PTPN12 enabled recognition of different HER2 phosphorylation sites and regulated specific PTPN12 functions. In addition, the structure of PTPN12 revealed a CDK2 phosphorylation site in a specific PTPN12 loop. Taken together, our results not only provide the working mechanisms of PTPN12 for desphosphorylation of its substrates but will also help in designing specific inhibitors of PTPN12.

PubMed: 27134172
DOI: 10.1016/j.celrep.2016.04.016

実験手法

X-RAY DIFFRACTION (2.043 Å)