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- W47123523 endingPage "166" @default.
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- W47123523 abstract "We have solved the crystal structures of the bacteriophage RB69 sliding clamp, its complex with a peptide essential for DNA polymerase interactions, and the DNA polymerase complexed with primer–template DNA. The editing complex structure shows a partially melted duplex DNA exiting from the exonuclease domain at an unexpected angle and significant changes in the protein structure. The clamp complex shows the C-terminal 11 residues of polymerase bound in a hydrophobic pocket, and it allows docking of the editing and clamp structures together. The peptide binds to the sliding clamp at a position identical to that of a replication inhibitor peptide bound to PCNA, suggesting that the replication inhibitor protein p21CIP1 functions by competing with eukaryotic polymerases for the same binding pocket on the clamp." @default.
- W47123523 created "2016-06-24" @default.
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- W47123523 creator A5068048009 @default.
- W47123523 date "1999-10-01" @default.
- W47123523 modified "2023-10-13" @default.
- W47123523 title "Building a Replisome from Interacting Pieces" @default.
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- W47123523 doi "https://doi.org/10.1016/s0092-8674(00)81647-5" @default.
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