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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Protein science : a publication of the Protein Society

Structural characterization of a pathogenic mutant of human protein tyrosine phosphatase PTPN2 (Cys216Gly) that causes very early onset autoimmune enteropathy.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Protein science : a publication of the Protein Society - 22 Nov 2021

Nian Q, Berthelet J, Parlato M, Mechaly AE, Liu R, Dupret JM, Cerf-Bensussan N, Haouz A, Rodrigues Lima F,

Link to Pubmed [PMID] – 34806245

Link to DOI – 10.1002/pro.4246

Protein Sci 2021 Nov; ():

PTPN2 is an important protein tyrosine phosphatase (PTP) that plays a key role in cell signaling. Deletions or inactivating mutations of PTPN2 have been described in different pathologies and underline its critical role in hematopoiesis, autoimmunity, and inflammation. Surprisingly, despite the major pathophysiological implications of PTPN2, the structural analysis of this PTP and notably of its pathogenic mutants remains poorly documented. Contrary to other human PTP enzymes, to date, only one structure of PTPN2 (wild-type form) has been reported. Here, we report the first crystal structure of a pathogenic mutant of PTPN2 (Cys216Gly) that causes an autoimmune enteropathy. We show in particular that this mutant adopts a classical PTP fold. More importantly, albeit inactive, the mutant retains its ability to bind substrates and to adopt the characteristic catalytically competent closed form of PTP enzymes. This novel PTPN2 structure may serve as a new tool to better understand PTP structures and the structural impacts of pathogenic mutations. Moreover, the C216G PTPN2 structure could also be helpful to design specific ligands/inhibitors.

https://pubmed.ncbi.nlm.nih.gov/34806245