1ul1: Difference between revisions

Revision as of 16:25, 21 February 2008

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 with as ligand. 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

Page seeded by OCA on Thu Feb 21 15:25:39 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 '''Crystal structure of the human FEN1-PCNA complex'''<br />
 ==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.
+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==
-UL1 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UL1 OCA].
+UL1 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==
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 [[Category: sliding clamp]]
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