2Y96

Structure of human dual-specificity phosphatase 27

Summary for 2Y96

Entry DOI	10.2210/pdb2y96/pdb
Descriptor	DUAL SPECIFICITY PHOSPHATASE DUPD1, SULFATE ION (3 entities in total)
Functional Keywords	hydrolase
Biological source	HOMO SAPIENS (HUMAN)
Cellular location	Cytoplasm: Q68J44
Total number of polymer chains	2
Total formula weight	51153.20
Authors	Lountos, G.T.,Tropea, J.E.,Waugh, D.S. (deposition date: 2011-02-11, release date: 2011-04-27, Last modification date: 2023-12-20)
Primary citation	Lountos, G.T.,Tropea, J.E.,Waugh, D.S. Structure of Human Dual-Specificity Phosphatase at 2.38A Resolution Acta Crystallogr.,Sect.D, 67:471-, 2011 Cited by PubMed Abstract: There are over 100 genes in the human genome that encode protein tyrosine phosphatases (PTPs) and approximately 60 of these are classified as dual-specificity phosphatases (DUSPs). Although many dual-specificity phosphatases are still not well characterized, novel functions have been discovered for some of them that have led to new insights into a variety of biological processes and the molecular basis for certain diseases. Indeed, as the functions of DUSPs continue to be elucidated, a growing number of them are emerging as potential therapeutic targets for diseases such as cancer, diabetes and inflammatory disorders. Here, the overexpression, purification and structure determination of DUSP27 at 2.38 Å resolution are presented. PubMed: 21543850 DOI: 10.1107/S090744491100970X PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.38 Å)

Structure validation