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| [[Image:1u76.gif|left|200px]] | | {{Seed}} |
| | [[Image:1u76.png|left|200px]] |
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| {{STRUCTURE_1u76| PDB=1u76 | SCENE= }} | | {{STRUCTURE_1u76| PDB=1u76 | SCENE= }} |
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| '''Crystal structure of hPCNA bound to residues 452-466 of the DNA polymerase-delta-p66 subunit'''
| | ===Crystal structure of hPCNA bound to residues 452-466 of the DNA polymerase-delta-p66 subunit=== |
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| ==Overview==
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| Human Proliferating Cellular Nuclear Antigen (hPCNA), a member of the sliding clamp family of proteins, makes specific protein-protein interactions with DNA replication and repair proteins through a small peptide motif termed the PCNA-interacting protein, or PIP-box. We solved the structure of hPCNA bound to PIP-box-containing peptides from the p66 subunit of the human replicative DNA polymerase-delta (452-466) at 2.6 A and of the flap endonuclease (FEN1) (331-350) at 1.85 A resolution. Both structures demonstrate that the pol-delta p66 and FEN1 peptides interact with hPCNA at the same site shown to bind the cdk-inhibitor p21(CIP1). Binding studies indicate that peptides from the p66 subunit of the pol-delta holoenzyme and FEN1 bind hPCNA from 189- to 725-fold less tightly than those of p21. Thus, the PIP-box and flanking regions provide a small docking peptide whose affinities can be readily adjusted in accord with biological necessity to mediate the binding of DNA replication and repair proteins to hPCNA.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15576034}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15576034 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15576034}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pip-box]] | | [[Category: Pip-box]] |
| [[Category: Sliding clamp]] | | [[Category: Sliding clamp]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:50:30 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:44:17 2008'' |