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5YCO

Complex structure of PCNA with UHRF2

Summary for 5YCO
Entry DOI10.2210/pdb5yco/pdb
DescriptorProliferating cell nuclear antigen, E3 ubiquitin-protein ligase UHRF2, GLYCEROL, ... (5 entities in total)
Functional Keywordscomplex structure, pcna, uhrf2, dna binding protein
Biological sourceHomo sapiens (Human)
More
Cellular locationNucleus : P12004 Q96PU4
Total number of polymer chains6
Total formula weight124603.02
Authors
Wu, M.,Chen, W.,Hang, T.,Wang, C.,Zhang, X.,Zang, J. (deposition date: 2017-09-07, release date: 2017-11-15, Last modification date: 2023-11-22)
Primary citationChen, W.,Wu, M.,Hang, T.,Wang, C.,Zhang, X.,Zang, J.
Structure insights into the molecular mechanism of the interaction between UHRF2 and PCNA.
Biochem. Biophys. Res. Commun., 494:575-580, 2017
Cited by
PubMed Abstract: UHRF2 (Ubiquitin-like with PHD and ring finger domains 2) is an E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications and cell cycle regulation by interacting with multiple epigenetic or cell-cycle related proteins. Previous studied have identified PCNA (Proliferating cell nuclear antigen) as an interacting partner of UHRF2 by using the antibody microarray. However, the molecular mechanism and the function of UHRF2-PCNA interaction remains unclear. Here, we report the complex structure of PCNA and the peptide (NEILQTLLDLFFPGYSK) derived from UHRF2 that contains a PIP box. Structural analysis combined with mutagenesis experiments provide the molecular basis for the recognition of UHRF2 by PCNA via PIP-box.
PubMed: 28951215
DOI: 10.1016/j.bbrc.2017.09.102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.199 Å)
Structure validation

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