8gvv | pdb_00008gvv

PTPN21 PTP domain C1108S mutant

spinqualitylabelsall models 8gvv, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8gvv is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: IOD, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PTN21_HUMAN Publication Abstract from PubMed PTPN21 belongs to the four-point-one, ezrin, radixin, moesin (FERM) domain-containing protein tyrosine phosphatases (PTP) and plays important roles in cytoskeleton-associated cellular processes like cell adhesion, motility, and cargo transport. Because of the presence of a WPE loop instead of a WPD loop in the phosphatase domain, it is often considered to lack phosphatase activity. However, many of PTPN21's biological functions require its catalytic activity. To reconcile these findings, we have determined the structures of individual PTPN21 FERM, PTP domains, and a complex between FERM-PTP. Combined with biochemical analysis, we have found that PTPN21 PTP is weakly active and is autoinhibited by association with its FERM domain. Disruption of FERM-PTP interaction results in enhanced ERK activation. The oncogenic HPV18 E7 protein binds to PTP at the same location as PTPN21 FERM, indicating that it may act by displacing the FERM domain from PTP. Our results provide mechanistic insight into PTPN21 and benefit functional studies of PTPN21-mediated processes. Structural analysis of PTPN21 reveals a dominant-negative effect of the FERM domain on its phosphatase activity.,Chen L, Qian Z, Zheng Y, Zhang J, Sun J, Zhou C, Xiao H Sci Adv. 2024 Mar;10(9):eadi7404. doi: 10.1126/sciadv.adi7404. Epub 2024 Feb 28. PMID:38416831 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosine phosphatase 3D structures

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