Atomistic ensemble of active SHP2 phosphatase.

Journal

Communications biology

ISSN: 2399-3642

Titre abrégé: Commun Biol

Pays: England

ID NLM: 101719179

Informations de publication

Date de publication:
21 Dec 2023

Historique:

received: 05 07 2023

accepted: 06 12 2023

medline: 22 12 2023

pubmed: 22 12 2023

entrez: 22 12 2023

Statut: epublish

Résumé

SHP2 phosphatase plays an important role in regulating several intracellular signaling pathways. Pathogenic mutations of SHP2 cause developmental disorders and are linked to hematological malignancies and cancer. SHP2 comprises two tandemly-arranged SH2 domains, a catalytic PTP domain, and a disordered C-terminal tail. Under physiological, non-stimulating conditions, the catalytic site of PTP is occluded by the N-SH2 domain, so that the basal activity of SHP2 is low. Whereas the autoinhibited structure of SHP2 has been known for two decades, its active, open structure still represents a conundrum. Since the oncogenic mutant SHP2

Identifiants

DOI: 10.1038/s42003-023-05682-5 PMID: 38129686

pubmed: 38129686

doi: 10.1038/s42003-023-05682-5

pii: 10.1038/s42003-023-05682-5

doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

Pagination

1289

Subventions

Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)

ID : HU 1971/3-1

Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)

ID : INST 256/539-1

Informations de copyright

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