2WGP

Crystal structure of human dual specificity phosphatase 14

Summary for 2WGP

• Entry DOI: 10.2210/pdb2wgp/pdb
• Descriptor: DUAL SPECIFICITY PROTEIN PHOSPHATASE 14, PHOSPHATE ION (3 entities in total)
• Functional Keywords: mkp6, dusp14, hydrolase, protein phosphatase, dual specificity phosphatase
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 42775.32

Authors

Lountos, G.T.,Tropea, J.E.,Cherry, S.,Waugh, D.S. (deposition date: 2009-04-22, release date: 2009-10-06, Last modification date: 2023-12-13)

Primary citation

Lountos, G.T.,Tropea, J.E.,Cherry, S.,Waugh, D.S.
Overproduction, Purification and Structure Determination of Human Dual-Specificity Phosphatase 14.
Acta Crystallogr.,Sect.D, 65:1013-, 2009

PubMed Abstract: Dual-specificity phosphatases (DUSPs) are enzymes that participate in the regulation of biological processes such as cell growth, differentiation, transcription and metabolism. A number of DUSPs are able to dephosphorylate phosphorylated serine, threonine and tyrosine residues on mitogen-activated protein kinases (MAPKs) and thus are also classified as MAPK phosphatases (MKPs). As an increasing number of DUSPs are being identified and characterized, there is a growing need to understand their biological activities at the molecular level. There is also significant interest in identifying DUSPs that could be potential targets for drugs that modulate MAPK-dependent signaling and immune responses, which have been implicated in a variety of maladies including cancer, infectious diseases and inflammatory disorders. Here, the overproduction, purification and crystal structure at 1.88 A resolution of human dual-specificity phosphatase 14, DUSP14 (MKP6), are reported. This structural information should accelerate the study of DUSP14 at the molecular level and may also accelerate the discovery and development of novel therapeutic agents.

PubMed: 19770498
DOI: 10.1107/S0907444909023762

Experimental method

X-RAY DIFFRACTION (1.88 Å)