8F5Q

Crystal structure of human PCNA in complex with the PIP box of FBH1

Summary for 8F5Q

• Entry DOI: 10.2210/pdb8f5q/pdb
• Descriptor: Proliferating cell nuclear antigen, F-box DNA helicase 1 (3 entities in total)
• Functional Keywords: complex, dna binding protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 89336.74

Authors

Liu, J.,Chaves-Arquero, B.,Wei, P.,Tencer, H.,Zhang, G.,Blanco, F.,Kutateladze, T. (deposition date: 2022-11-15, release date: 2023-09-27, Last modification date: 2024-10-16)

Primary citation

Liu, J.,Chaves-Arquero, B.,Wei, P.,Tencer, A.H.,Ruiz-Albor, A.,Zhang, G.,Blanco, F.J.,Kutateladze, T.G.
Molecular insight into the PCNA-binding mode of FBH1.
Structure, 31:511-517.e3, 2023

PubMed Abstract: F-box DNA helicase 1 (FBH1) is involved in the regulation of cell responses to replicative stress. FBH1 is recruited to stalled DNA replication fork by PCNA where it inhibits homologous recombination and catalyzes fork regression. Here, we report the structural basis for the molecular recognition of two distinctly different motifs of FBH1, FBH1 and FBH1, by PCNA. The crystal structure of PCNA in complex with FBH1 and analysis of NMR perturbations reveal overlapped FBH1 and FBH1 binding sites of PCNA and the dominant contribution of FBH1 in this interaction.

PubMed: 36990095
DOI: 10.1016/j.str.2023.03.004

Experimental method

X-RAY DIFFRACTION (1.9 Å)