1u76: Difference between revisions

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{{STRUCTURE_1u76|  PDB=1u76  |  SCENE=  }}  
{{STRUCTURE_1u76|  PDB=1u76  |  SCENE=  }}  


'''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===




==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.
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{{ABSTRACT_PUBMED_15576034}}


==About this Structure==
==About this Structure==
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[[Category: Pip-box]]
[[Category: Pip-box]]
[[Category: Sliding clamp]]
[[Category: Sliding clamp]]
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