STRUCTURE OF THE C-TERMINAL REGION OF P21(WAF1 CIP1) COMPLEXED WITH HUMAN PCNA/

Citation
Jm. Gulbis et al., STRUCTURE OF THE C-TERMINAL REGION OF P21(WAF1 CIP1) COMPLEXED WITH HUMAN PCNA/, Cell, 87(2), 1996, pp. 297-306
Citations number
47
Categorie Soggetti
Biology,"Cell Biology
Journal title
CellACNP
ISSN journal
00928674
Volume
87
Issue
2
Year of publication
1996
Pages
297 - 306
Database
ISI
SICI code
0092-8674(1996)87:2<297:SOTCRO>2.0.ZU;2-E
Abstract
The crystal structure of the human DNA polymerase delta processivity f actor PCNA (proliferating cell nuclear antigen) complexed with a 22 re sidue peptide derived from the C-terminus of the cell-cycle checkpoint protein p21(WAF1/CIP1) has been determined at 2.6 Angstrom resolution . p21 binds to PCNA in a 1:1 stoichiometry with an extensive array of interactions that include the formation of a beta sheet with the inter domain connector loop of PCNA. An intact trimeric ring is maintained i n 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 as sembly.