scholarly journals Crystal structure of the human dual specificity phosphatase 1 catalytic domain

2017 ◽  
Vol 27 (2) ◽  
pp. 561-567 ◽  
Author(s):  
Rajesh Gumpena ◽  
George T. Lountos ◽  
Sreejith Raran-Kurussi ◽  
Joseph E. Tropea ◽  
Scott Cherry ◽  
...  
2013 ◽  
Vol 69 (6) ◽  
pp. 1160-1170 ◽  
Author(s):  
Eun-Young Won ◽  
Yong Xie ◽  
Chie Takemoto ◽  
Lirong Chen ◽  
Zhi-Jie Liu ◽  
...  

Author(s):  
George T. Lountos ◽  
Scott Cherry ◽  
Joseph E. Tropea ◽  
David S. Waugh

4-Nitrophenyl phosphate (p-nitrophenyl phosphate, pNPP) is widely used as a small molecule phosphotyrosine-like substrate in activity assays for protein tyrosine phosphatases. It is a colorless substrate that upon hydrolysis is converted to a yellow 4-nitrophenolate ion that can be monitored by absorbance at 405 nm. Therefore, the pNPP assay has been widely adopted as a quick and simple method to assess phosphatase activity and is also commonly used in assays to screen for inhibitors. Here, the first crystal structure is presented of a dual-specificity phosphatase, human dual-specificity phosphatase 22 (DUSP22), in complex with pNPP. The structure illuminates the molecular basis for substrate binding and may also facilitate the structure-assisted development of DUSP22 inhibitors.


Author(s):  
George T. Lountos ◽  
Brian P. Austin ◽  
Joseph E. Tropea ◽  
David S. Waugh

Human dual-specificity phosphatase 7 (DUSP7/Pyst2) is a 320-residue protein that belongs to the mitogen-activated protein kinase phosphatase (MKP) subfamily of dual-specificity phosphatases. Although its precise biological function is still not fully understood, previous reports have demonstrated that DUSP7 is overexpressed in myeloid leukemia and other malignancies. Therefore, there is interest in developing DUSP7 inhibitors as potential therapeutic agents, especially for cancer. Here, the purification, crystallization and structure determination of the catalytic domain of DUSP7 (Ser141–Ser289/C232S) at 1.67 Å resolution are reported. The structure described here provides a starting point for structure-assisted inhibitor-design efforts and adds to the growing knowledge base of three-dimensional structures of the dual-specificity phosphatase family.


2006 ◽  
Vol 66 (2) ◽  
pp. 272-278 ◽  
Author(s):  
Takehiro Yokota ◽  
Yukinori Nara ◽  
Akiko Kashima ◽  
Keiko Matsubara ◽  
Satoru Misawa ◽  
...  

2005 ◽  
Vol 61 (3) ◽  
pp. 694-697 ◽  
Author(s):  
Tae-Sung Yoon ◽  
Dae Gwin Jeong ◽  
Jae Hoon Kim ◽  
Yoon Hea Cho ◽  
Jeong Hee Son ◽  
...  

2006 ◽  
Vol 66 (1) ◽  
pp. 253-258 ◽  
Author(s):  
Dae Gwin Jeong ◽  
Yoon Hea Cho ◽  
Tae-Sung Yoon ◽  
Jae Hoon Kim ◽  
Seong Eon Ryu ◽  
...  

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