Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA Journal Article
| Authors: | Gulbis, J. M.; Kelman, Z.; Hurwitz, J.; O'Donnell, M.; Kuriyan, J. |
| Article Title: | Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA |
| Abstract: | The crystal structure of the human DNA polymerase δ processivity factor PCNA (proliferating cell nuclear antigen) complexed with a 22 residue peptide derived from the C-terminus of the cell-cycle checkpoint protein p21(WAF1/CIP1) has been determined at 2.6 Å resolution. p21 binds to PCNA in a 1:1 stoichiometry with an extensive array of interactions that include the formation of a β sheet with the interdomain connector loop of PCNA. An intact trimeric ring is maintained in the structure of the p21-PCNA complex, with a central hole available for DNA interaction. The ability of p21 to inhibit the action of PCNA is therefore likely to be due to its masking of elements on PCNA that are required for the binding of other components of the polymerase assembly. |
| Keywords: | nonhuman; dna polymerase; dna replication; carboxy terminal sequence; protein protein interaction; crystal structure; hydrogen bond; cycline; protein p21; electric potential; hydrophobicity; human; priority journal; article |
| Journal Title: | Cell |
| Volume: | 87 |
| Issue: | 2 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 1996-10-18 |
| Start Page: | 297 |
| End Page: | 306 |
| Language: | English |
| DOI: | 10.1016/s0092-8674(00)81347-1 |
| PUBMED: | 8861913 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 22 November 2017 -- Source: Scopus |
