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Overproduction, purification and structure determination of human dual-specificity phosphatase 14

机译:生产过剩,净化和结构测定人类dual-specificity磷酸酶14

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摘要

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 phosphoryl-ated 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 ? 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.
机译:Dual-specificity磷酸酶(DUSPs)的酶参与调节的生物过程,如细胞生长、分化、转录和新陈代谢。可以脱去磷酸phosphoryl-ated吗丝氨酸、苏氨酸和酪氨酸残基增殖蛋白激酶(MAPKs)和因此也被归类为MAPK磷酸酶(MKPs)。被识别和特征,有一个越来越需要了解他们的生物在分子水平上的活动。识别DUSPs感兴趣可能是潜在目标药物吗调节MAPK-dependent信号和免疫反应,已涉及多种疾病,包括癌症、传染性疾病和炎症性疾病。生产过剩、净化和晶体结构在1.88吗?DUSP14 dual-specificity磷酸酶14日(MKP6),报告。加速DUSP14在分子的研究水平,也可能加速发现开发新型治疗药物。

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