1ul1

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[[Image:1ul1.gif|left|200px]]
[[Image:1ul1.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1ul1", creates the "Structure Box" on the page.
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{{STRUCTURE_1ul1| PDB=1ul1 | SCENE= }}
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|RELATEDENTRY=[[1b43|1B43]], [[1a76|1A76]], [[1axc|1AXC]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ul1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ul1 OCA], [http://www.ebi.ac.uk/pdbsum/1ul1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ul1 RCSB]</span>
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'''Crystal structure of the human FEN1-PCNA complex'''
'''Crystal structure of the human FEN1-PCNA complex'''
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[[Category: Uchida, M.]]
[[Category: Uchida, M.]]
[[Category: Yamaguchi, H.]]
[[Category: Yamaguchi, H.]]
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[[Category: dna clamp]]
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[[Category: Dna clamp]]
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[[Category: dna repair]]
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[[Category: Dna repair]]
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[[Category: dna-binding protein]]
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[[Category: Dna-binding protein]]
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[[Category: flap dna]]
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[[Category: Flap dna]]
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[[Category: flap endonuclease]]
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[[Category: Flap endonuclease]]
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[[Category: hydrolase/dna binding protein complex]]
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[[Category: Hydrolase/dna binding protein complex]]
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[[Category: protein complex]]
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[[Category: Protein complex]]
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[[Category: replication]]
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[[Category: Replication]]
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[[Category: sliding clamp]]
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[[Category: Sliding clamp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:22:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:11:43 2008''
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Revision as of 08:22, 3 May 2008

Image:1ul1.gif

Template:STRUCTURE 1ul1

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. 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 Sat May 3 11:22:22 2008

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OCA

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