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| {{STRUCTURE_1ul1| PDB=1ul1 | SCENE= }} | | {{STRUCTURE_1ul1| PDB=1ul1 | SCENE= }} |
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| '''Crystal structure of the human FEN1-PCNA complex'''
| | ===Crystal structure of the human FEN1-PCNA complex=== |
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| ==Overview==
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| Flap endonuclease-1 (FEN1) is a key enzyme for maintaining genomic stability and replication. Proliferating cell nuclear antigen (PCNA) binds FEN1 and stimulates its endonuclease activity. The structural basis of the FEN1-PCNA interaction was revealed by the crystal structure of the complex between human FEN1 and PCNA. The main interface involves the C-terminal tail of FEN1, which forms two beta-strands connected by a short helix, the betaA-alphaA-betaB motif, participating in beta-beta and hydrophobic interactions with PCNA. These interactions are similar to those previously observed for the p21CIP1/WAF1 peptide. However, this structure involving the full-length enzyme has revealed additional interfaces that are involved in the core domain. The interactions at the interfaces maintain the enzyme in an inactive 'locked-down' orientation and might be utilized in rapid DNA-tracking by preserving the central hole of PCNA for sliding along the DNA. A hinge region present between the core domain and the C-terminal tail of FEN1 would play a role in switching the FEN1 orientation from an inactive to an active orientation.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15616578}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15616578 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15616578}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Replication]] | | [[Category: Replication]] |
| [[Category: Sliding clamp]] | | [[Category: Sliding clamp]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:22:22 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:12:57 2008'' |
