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1ul1
From Proteopedia
(New page: 200px<br /> <applet load="1ul1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ul1, resolution 2.9Å" /> '''Crystal structure of...) |
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| - | [[Image:1ul1.gif|left|200px]]<br /> | + | [[Image:1ul1.gif|left|200px]]<br /><applet load="1ul1" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ul1" size=" | + | |
caption="1ul1, resolution 2.9Å" /> | caption="1ul1, resolution 2.9Å" /> | ||
'''Crystal structure of the human FEN1-PCNA complex'''<br /> | '''Crystal structure of the human FEN1-PCNA complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Flap endonuclease-1 (FEN1) is a key enzyme for maintaining genomic | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1UL1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1UL1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UL1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sliding clamp]] | [[Category: sliding clamp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:39 2008'' |
Revision as of 13:25, 21 February 2008
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Crystal structure of the human FEN1-PCNA complex
Overview
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.
About this Structure
1UL1 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for recruitment of human flap endonuclease 1 to PCNA., Sakurai S, Kitano K, Yamaguchi H, Hamada K, Okada K, Fukuda K, Uchida M, Ohtsuka E, Morioka H, Hakoshima T, EMBO J. 2005 Feb 23;24(4):683-93. Epub 2004 Dec 16. PMID:15616578
Page seeded by OCA on Thu Feb 21 15:25:39 2008
Categories: Homo sapiens | Protein complex | Fukuda, K. | Hakoshima, T. | Hamada, K. | Kitano, K. | Morioka, H. | Ohtsuka, E. | Okada, K. | Sakurai, S. | Uchida, M. | Yamaguchi, H. | MG | Dna clamp | Dna repair | Dna-binding protein | Flap dna | Flap endonuclease | Hydrolase/dna binding protein complex | Replication | Sliding clamp
