6K3A
Crystal structure of human PCNA in complex with DNMT1 PIP box motif.
Summary for 6K3A
| Entry DOI | 10.2210/pdb6k3a/pdb |
| Descriptor | Proliferating cell nuclear antigen, Peptide from DNA (cytosine-5)-methyltransferase 1 (3 entities in total) |
| Functional Keywords | dnmt1, pcna, dna methylation, pip box, replication |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 93676.56 |
| Authors | Jimenji, T.,Kori, S.,Arita, K. (deposition date: 2019-05-17, release date: 2019-06-26, Last modification date: 2023-11-22) |
| Primary citation | Jimenji, T.,Matsumura, R.,Kori, S.,Arita, K. Structure of PCNA in complex with DNMT1 PIP box reveals the basis for the molecular mechanism of the interaction. Biochem.Biophys.Res.Commun., 516:578-583, 2019 Cited by PubMed Abstract: DNMT1 is a C5-DNA methyltransferase that plays a pivotal role in DNA methylation maintenance. During early and mid S-phase, DNMT1 accumulates at DNA replication sites by binding to proliferating cell nuclear antigen (PCNA), an essential factor for DNA replication, through a PIP box motif. However, the molecular mechanism by which the DNMT1 PIP box motif binds to PCNA remains unclear. Here, we report the crystal structure of PCNA bound to DNMT1 PIP box peptide. The structure reveals the detailed interaction between PCNA and DNMT1 PIP box; conserved glutamine and hydrophobic/aromatic residues in the PIP box are recognized by the Q- and hydrophobic pockets of PCNA, respectively. The structure also shows novel intramolecular interactions within the PIP box motif, which stabilize the helix conformation in the PIP box. Our data provide structural insight into the recruitment of DNMT1 to replication sites by PCNA. PubMed: 31235252DOI: 10.1016/j.bbrc.2019.06.060 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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