5IY4
Crystal structure of human PCNA in complex with the PIP box of DVC1
Summary for 5IY4
Entry DOI | 10.2210/pdb5iy4/pdb |
Descriptor | Proliferating cell nuclear antigen, DVC1 PIP box (2 entities in total) |
Functional Keywords | pcna, pip box, dvc1, dna binding protein |
Biological source | Homo sapiens (Human) More |
Cellular location | Nucleus : P12004 |
Total number of polymer chains | 6 |
Total formula weight | 95568.07 |
Authors | |
Primary citation | Wang, 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: 27084448DOI: 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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