1ul1: Difference between revisions
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|PDB= 1ul1 |SIZE=350|CAPTION= <scene name='initialview01'>1ul1</scene>, resolution 2.9Å | |PDB= 1ul1 |SIZE=350|CAPTION= <scene name='initialview01'>1ul1</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1b43|1B43]], [[1a76|1A76]], [[1axc|1AXC]] | |||
|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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[[Category: Uchida, M.]] | [[Category: Uchida, M.]] | ||
[[Category: Yamaguchi, H.]] | [[Category: Yamaguchi, H.]] | ||
[[Category: dna clamp]] | [[Category: dna clamp]] | ||
[[Category: dna repair]] | [[Category: dna repair]] | ||
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[[Category: sliding clamp]] | [[Category: sliding clamp]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:11:43 2008'' | ||
Revision as of 00:11, 31 March 2008
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| , resolution 2.9Å | |||||||
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| Ligands: | |||||||
| Related: | 1B43, 1A76, 1AXC
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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