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. 2008 Oct 1;64(Pt 10):954-6.
doi: 10.1107/S1744309108028522. Epub 2008 Sep 30.

Initial crystallographic study of human PCNA in complex with a peptide containing the noncanonical PIP-box sequence of human DNA polymerase iota

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Initial crystallographic study of human PCNA in complex with a peptide containing the noncanonical PIP-box sequence of human DNA polymerase iota

Asami Hishiki et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

Human DNA polymerase iota (Poliota) is one of the Y-family DNA polymerases involved in translesion synthesis (TLS), which allows continued replication at damaged DNA templates. Poliota has a noncanonical PCNA-interacting protein box (PIP-box) within an internal region of the protein. Poliota activity is stimulated by PCNA binding through the noncanonical PIP-box. To clarify the interaction of PCNA with the noncanonical PIP-box of Poliota, PCNA and a Poliota peptide carrying the noncanonical PIP-box complex have been cocrystallized. The crystal belongs to space group C2, with unit-cell parameters a = 167.1, b = 68.7, c = 90.0 A, beta = 95.1 degrees . Structural analysis by molecular replacement is in progress.

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Figures

Figure 1
Figure 1
Crystals of the PCNA–Polι peptide complex.
Figure 2
Figure 2
A diffraction pattern from a crystal of the PCNA–Polι peptide complex.

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