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PDBsum entry 2wgp

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Hydrolase PDB id
2wgp
Jmol
Contents
Protein chain
168 a.a.
Ligands
PO4 ×2
Waters ×347

References listed in PDB file
Key reference
Title Overproduction, Purification and structure determination of human dual-Specificity phosphatase 14.
Authors G.T.Lountos, J.E.Tropea, S.Cherry, D.S.Waugh.
Ref. Acta Crystallogr D Biol Crystallogr, 2009, 65, 1013-1020. [DOI no: 10.1107/S0907444909023762]
PubMed id 19770498
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.
Figure 2.
Figure 2 Ribbon representation of the three-dimensional structure of monomeric DUSP14.
Figure 6.
Figure 6 Stereoview of the superimposed coordinates of DUSP14 (PDB code 2wgp ; cyan) and DUSP18 (PDB code 2esb ; red).
The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2009, 65, 1013-1020) copyright 2009.
Secondary reference #1
Title Negative-Feedback regulation of cd28 costimulation by a novel mitogen-Activated protein kinase phosphatase, Mkp6.
Authors F.Marti, A.Krause, N.H.Post, C.Lyddane, B.Dupont, M.Sadelain, P.D.King.
Ref. J Immunol, 2001, 166, 197-206.
PubMed id 11123293
Abstract
PROCHECK
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