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Article

Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases.

International journal of molecular sciences - 12 Oct 2020

Lai Chih-Hsuan, Chang Co-Chih, Chuang Huai-Chia, Tan Tse-Hua, Lyu Ping-Chiang

Abstract excerpt

Cysteine-based protein tyrosine phosphatases (Cys-based PTPs) perform dephosphorylation to regulate signaling pathways in cellular responses. The hydrogen bonding network in their active site plays an important conformational role and supports the phosphatase activity. Nearly half of dual-specificity phosphatases (DUSPs) use three conserved residues, including aspartate in the D-loop, serine in the P-loop, and...

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Identifiers

PMID: 33053837
DOI: 10.3390/ijms21207515
PMCID: PMC7589817

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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