1ul1: Difference between revisions
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[[Image:1ul1.gif|left|200px]] | [[Image:1ul1.gif|left|200px]] | ||
'''Crystal structure of the human FEN1-PCNA complex''' | {{Structure | ||
|PDB= 1ul1 |SIZE=350|CAPTION= <scene name='initialview01'>1ul1</scene>, resolution 2.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of the human FEN1-PCNA complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1UL1 is a [ | 1UL1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UL1 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15616578 15616578] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: sliding clamp]] | [[Category: sliding clamp]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:33:21 2008'' | ||
Revision as of 15:33, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the human FEN1-PCNA complex
OverviewOverview
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 StructureAbout this Structure
1UL1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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