{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Garrido-Urbani S"],"funding":["Åke Wiberg Stiftelse","Vetenskapsrådet","Institut National de la Santé et de la Recherche Médicale","Canadian Institutes of Health Research"],"pagination":["3-12"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4819696"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["590(1)"],"pubmed_abstract":["Syntenin has crucial roles in cell adhesion, cell migration and synaptic transmission. Its closely linked postsynaptic density-95, discs large 1, zonula occludens-1 (PDZ) domains typically interact with C-terminal ligands. We profile syntenin PDZ1-2 through proteomic peptide phage display (ProP-PD) using a library that displays C-terminal regions of the human proteome. The protein recognizes a broad range of peptides, with a preference for hydrophobic motifs and has a tendency to recognize cryptic internal ligands. We validate the interaction with nectin-1 through orthogonal assays. The study demonstrates the power of ProP-PD as a complementary approach to uncover interactions of potential biological relevance."],"journal":["FEBS letters"],"pubmed_title":["Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin."],"pmcid":["PMC4819696"],"funding_grant_id":["MOP-93684","3773397","C0509201"],"pubmed_authors":["Zimmermann P","Lopez M","Lembo F","Sidhu SS","Sundell GN","Ghossoub R","Arnold R","Garrido-Urbani S","Garg P","Kim PM","Ivarsson Y"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin.","description":"Syntenin has crucial roles in cell adhesion, cell migration and synaptic transmission. Its closely linked postsynaptic density-95, discs large 1, zonula occludens-1 (PDZ) domains typically interact with C-terminal ligands. We profile syntenin PDZ1-2 through proteomic peptide phage display (ProP-PD) using a library that displays C-terminal regions of the human proteome. The protein recognizes a broad range of peptides, with a preference for hydrophobic motifs and has a tendency to recognize cryptic internal ligands. We validate the interaction with nectin-1 through orthogonal assays. The study demonstrates the power of ProP-PD as a complementary approach to uncover interactions of potential biological relevance.","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jan","modification":"2026-04-07T17:12:32.797Z","creation":"2019-03-27T03:11:08Z"},"accession":"S-EPMC4819696","cross_references":{"pubmed":["26787460"],"doi":["10.1002/1873-3468.12037"]}}