1U76

Crystal structure of hPCNA bound to residues 452-466 of the DNA polymerase-delta-p66 subunit

Summary for 1U76

• Entry DOI: 10.2210/pdb1u76/pdb
• Related: 1u7b
• Descriptor: Proliferating cell nuclear antigen, KANRQVSITGFFQRK peptide from DNA polymerase delta subunit 3 (3 entities in total)
• Functional Keywords: dna replication, sliding clamp, dna polymerase delta, p66, pip-box, replication
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P12004 Q15054
• Total number of polymer chains: 6
• Total formula weight: 91739.47

Authors

Bruning, J.B.,Shamoo, Y. (deposition date: 2004-08-02, release date: 2004-12-14, Last modification date: 2023-08-23)

Primary citation

Bruning, J.B.,Shamoo, Y.
Structural and Thermodynamic Analysis of Human PCNA with Peptides Derived from DNA Polymerase-delta p66 Subunit and Flap Endonuclease-1.
Structure, 12:2209-2219, 2004

PubMed Abstract: Human Proliferating Cellular Nuclear Antigen (hPCNA), a member of the sliding clamp family of proteins, makes specific protein-protein interactions with DNA replication and repair proteins through a small peptide motif termed the PCNA-interacting protein, or PIP-box. We solved the structure of hPCNA bound to PIP-box-containing peptides from the p66 subunit of the human replicative DNA polymerase-delta (452-466) at 2.6 A and of the flap endonuclease (FEN1) (331-350) at 1.85 A resolution. Both structures demonstrate that the pol-delta p66 and FEN1 peptides interact with hPCNA at the same site shown to bind the cdk-inhibitor p21(CIP1). Binding studies indicate that peptides from the p66 subunit of the pol-delta holoenzyme and FEN1 bind hPCNA from 189- to 725-fold less tightly than those of p21. Thus, the PIP-box and flanking regions provide a small docking peptide whose affinities can be readily adjusted in accord with biological necessity to mediate the binding of DNA replication and repair proteins to hPCNA.

PubMed: 15576034
DOI: 10.1016/j.str.2004.09.018

Experimental method

X-RAY DIFFRACTION (2.6 Å)