{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hara K"],"funding":["Naito Foundation","Takeda Science Foundation","Ministry of Education, Culture, Sports, Science and Technology","Japan Society for the Promotion of Science"],"pagination":["214-221"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5893992"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["74(Pt 4)"],"pubmed_abstract":["Proliferating cell nuclear antigen (PCNA) provides a molecular platform for numerous protein-protein interactions in DNA metabolism. A large number of proteins associated with PCNA have a well characterized sequence termed the PCNA-interacting protein box motif (PIPM). Another PCNA-interacting sequence termed the AlkB homologue 2 PCNA-interacting motif (APIM), comprising the five consensus residues (K/R)-(F/Y/W)-(L/I/V/A)-(L/I/V/A)-(K/R), has also been identified in various proteins. In contrast to that with PIPM, the PCNA-APIM interaction is less well understood. Here, the crystal structure of PCNA bound to a peptide carrying an APIM consensus sequence, RFLVK, was determined and structure-based interaction analysis was performed. The APIM peptide binds to the PIPM-binding pocket on PCNA in a similar way to PIPM. The phenylalanine and leucine residues within the APIM consensus sequence and a hydrophobic residue that precedes the APIM consensus sequence are crucially involved in interactions with the hydrophobic pocket of PCNA. This interaction is essential for overall binding. These results provide a structural basis for regulation of the PCNA interaction and might aid in the development of specific inhibitors of this interaction."],"journal":["Acta crystallographica. Section F, Structural biology communications"],"pubmed_title":["Structure of proliferating cell nuclear antigen (PCNA) bound to an APIM peptide reveals the universality of PCNA interaction."],"pmcid":["PMC5893992"],"funding_grant_id":["17H06014","15K18491","16H04755","17K07314","25291017"],"pubmed_authors":["Uchida M","Yokoyama H","Ishikawa Y","Tagata R","Hara K","Hishiki A","Hashimoto H"],"additional_accession":[]},"is_claimable":false,"name":"Structure of proliferating cell nuclear antigen (PCNA) bound to an APIM peptide reveals the universality of PCNA interaction.","description":"Proliferating cell nuclear antigen (PCNA) provides a molecular platform for numerous protein-protein interactions in DNA metabolism. A large number of proteins associated with PCNA have a well characterized sequence termed the PCNA-interacting protein box motif (PIPM). Another PCNA-interacting sequence termed the AlkB homologue 2 PCNA-interacting motif (APIM), comprising the five consensus residues (K/R)-(F/Y/W)-(L/I/V/A)-(L/I/V/A)-(K/R), has also been identified in various proteins. In contrast to that with PIPM, the PCNA-APIM interaction is less well understood. Here, the crystal structure of PCNA bound to a peptide carrying an APIM consensus sequence, RFLVK, was determined and structure-based interaction analysis was performed. The APIM peptide binds to the PIPM-binding pocket on PCNA in a similar way to PIPM. The phenylalanine and leucine residues within the APIM consensus sequence and a hydrophobic residue that precedes the APIM consensus sequence are crucially involved in interactions with the hydrophobic pocket of PCNA. This interaction is essential for overall binding. These results provide a structural basis for regulation of the PCNA interaction and might aid in the development of specific inhibitors of this interaction.","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Apr","modification":"2024-11-11T20:27:47.082Z","creation":"2020-05-22T14:54:31Z"},"accession":"S-EPMC5893992","cross_references":{"pubmed":["29633969"],"doi":["10.1107/S2053230X18003242","10.1107/s2053230x18003242"]}}