[HTML][HTML] Structure of the C-terminal region of p21WAF1/CIP1 complexed with human PCNA
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 …
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 …
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 p21WAF1/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.
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