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5IY4

Crystal structure of human PCNA in complex with the PIP box of DVC1

Summary for 5IY4
Entry DOI10.2210/pdb5iy4/pdb
DescriptorProliferating cell nuclear antigen, DVC1 PIP box (2 entities in total)
Functional Keywordspcna, pip box, dvc1, dna binding protein
Biological sourceHomo sapiens (Human)
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Cellular locationNucleus : P12004
Total number of polymer chains6
Total formula weight95568.07
Authors
Jiang, T.,Xu, M.,Wang, Y. (deposition date: 2016-03-24, release date: 2016-06-08, Last modification date: 2024-10-30)
Primary citationWang, Y.,Xu, M.,Jiang, T.
Crystal structure of human PCNA in complex with the PIP box of DVC1
Biochem.Biophys.Res.Commun., 474:264-270, 2016
Cited by
PubMed Abstract: In higher eukaryotes, DVC1 (SPRTN, Spartan or C1orf124) is implicated in the translesion synthesis (TLS) pathway. DVC1 localizes to sites of DNA damage, binds to the proliferating cell nuclear antigen (PCNA) via its conserved PCNA-interacting motif (PIP box), and associates with ubiquitin selective segregase p97 and other factors, thus regulating translesion synthesis polymerases. Here, we report the crystal structure of human PCNA in complex with a peptide ((321)SNSHQNVLSNYFPRVS(336)) derived from human DVC1 that contains a unique YF type PIP box. Structural analysis reveals the detailed PIP box-PCNA interaction. Interestingly, substitution of Y331 with Phe severely reduces its PCNA binding affinity. These findings offer new insights into the determinants of PIP box for PCNA binding.
PubMed: 27084448
DOI: 10.1016/j.bbrc.2016.04.053
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.945 Å)
Structure validation

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