Structural highlights
Function
MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.DUS1_HUMAN Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle.[UniProtKB:P28563]
Publication Abstract from PubMed
The dual specificity phosphatase DUSP1 was the first mitogen activated protein kinase phosphatase (MKP) to be identified. It dephosphorylates conserved tyrosine and threonine residues in the activation loops of mitogen activated protein kinases ERK2, JNK1 and p38-alpha. Here, we report the crystal structure of the human DUSP1 catalytic domain at 2.49 A resolution. Uniquely, the protein was crystallized as an MBP fusion protein in complex with a monobody that binds to MBP. Sulfate ions occupy the phosphotyrosine and putative phosphothreonine binding sites in the DUSP1 catalytic domain. This article is protected by copyright. All rights reserved.
Crystal structure of the human dual specificity phosphatase 1 catalytic domain.,Gumpena R, Lountos GT, Raran-Kurussi S, Tropea JE, Cherry S, Waugh DS Protein Sci. 2017 Oct 20. doi: 10.1002/pro.3328. PMID:29052270[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gumpena R, Lountos GT, Raran-Kurussi S, Tropea JE, Cherry S, Waugh DS. Crystal structure of the human dual specificity phosphatase 1 catalytic domain. Protein Sci. 2017 Oct 20. doi: 10.1002/pro.3328. PMID:29052270 doi:http://dx.doi.org/10.1002/pro.3328
