4.0 Article

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

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309108028522

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Funding

  1. Japan Society for the Promotion of Science (JSPS) [16770080, 18770091]
  2. Ministry of Education, Culture, Sports, Science and Technology (MEXT) [16048226, 17048023, 19036025, 17054035, 18054026, 20051020]
  3. National Project on Protein Structural and Functional Analyses [Protein 3000]
  4. Target Protein Research Program
  5. Grants-in-Aid for Scientific Research [20051020, 16048226, 17054035, 19036025, 16770080, 18770091, 18054026, 17048023] Funding Source: KAKEN

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Human DNA polymerase iota (Pol iota) is one of the Y-family DNA polymerases involved in translesion synthesis (TLS), which allows continued replication at damaged DNA templates. Pol iota has a noncanonical PCNA-interacting protein box (PIP-box) within an internal region of the protein. Pol iota activity is stimulated by PCNA binding through the noncanonical PIP-box. To clarify the interaction of PCNA with the noncanonical PIP-box of Pol iota, PCNA and a Pol iota 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 angstrom, beta = 95.1 degrees. Structural analysis by molecular replacement is in progress.

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