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Article

Structural mechanism associated with domain opening in gain-of-function mutations in SHP2 phosphatase.

Proteins - 1 May 2011

Darian Eva, Guvench Olgun, Yu Bing, Qu Cheng-Kui, MacKerell Alexander D

Abstract excerpt

The SHP2 phosphatase plays a central role in a number of signaling pathways were it dephosphorylates various substrate proteins. Regulation of SHP2 activity is, in part, achieved by an intramolecular interaction between the PTP domain of the protein, which contains the catalytic site, and the N-SH2 domain leading to a "closed" protein conformation and autoinhibition. Accordingly, "opening" of the N-SH2 and PTP...

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Identifiers

PMID: 21365683
DOI: 10.1002/prot.22984
PMCID: PMC3076527

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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