Sandbox 5: Difference between revisions
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<applet load='1axc' size='300' frame='true' align='right' caption='Insert caption here' /> | <applet load='1axc' size='300' frame='true' align='right' caption='Insert caption here' /> | ||
The crystal structure of the human DNA polymerase delta processivity factor | The crystal structure of the human DNA polymerase delta processivity factor name='Sandbox_5/Pcna/4'>TextToBeDisplayed</scene> | ||
(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 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 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. | (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 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 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. | ||
Flap endonuclease-1 (FEN1) is a key enzyme for maintaining genomic stability and replication. FEN1-PCNA interactions are similar to those previously observed for the p21CIP1/WAF1 peptide. | Flap endonuclease-1 (FEN1) is a key enzyme for maintaining genomic stability and replication. FEN1-PCNA interactions are similar to those previously observed for the p21CIP1/WAF1 peptide. | ||
Revision as of 10:22, 27 May 2008
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The crystal structure of the human DNA polymerase delta processivity factor name='Sandbox_5/Pcna/4'>TextToBeDisplayed</scene> (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 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 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. Flap endonuclease-1 (FEN1) is a key enzyme for maintaining genomic stability and replication. FEN1-PCNA interactions are similar to those previously observed for the p21CIP1/WAF1 peptide.