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2WGP

Crystal structure of human dual specificity phosphatase 14

2WGP の概要
エントリーDOI10.2210/pdb2wgp/pdb
分子名称DUAL SPECIFICITY PROTEIN PHOSPHATASE 14, PHOSPHATE ION (3 entities in total)
機能のキーワードmkp6, dusp14, hydrolase, protein phosphatase, dual specificity phosphatase
由来する生物種HOMO SAPIENS (HUMAN)
タンパク質・核酸の鎖数2
化学式量合計42775.32
構造登録者
Lountos, G.T.,Tropea, J.E.,Cherry, S.,Waugh, D.S. (登録日: 2009-04-22, 公開日: 2009-10-06, 最終更新日: 2023-12-13)
主引用文献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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.88 Å)
構造検証レポート
Validation report summary of 2wgp
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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