<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Garrido-Urbani S</submitter><funding>Åke Wiberg Stiftelse</funding><funding>Vetenskapsrådet</funding><funding>Institut National de la Santé et de la Recherche Médicale</funding><funding>Canadian Institutes of Health Research</funding><pagination>3-12</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4819696</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>590(1)</volume><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.</pubmed_abstract><journal>FEBS letters</journal><pubmed_title>Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin.</pubmed_title><pmcid>PMC4819696</pmcid><funding_grant_id>MOP-93684</funding_grant_id><funding_grant_id>3773397</funding_grant_id><funding_grant_id>C0509201</funding_grant_id><pubmed_authors>Zimmermann P</pubmed_authors><pubmed_authors>Lopez M</pubmed_authors><pubmed_authors>Lembo F</pubmed_authors><pubmed_authors>Sidhu SS</pubmed_authors><pubmed_authors>Sundell GN</pubmed_authors><pubmed_authors>Ghossoub R</pubmed_authors><pubmed_authors>Arnold R</pubmed_authors><pubmed_authors>Garrido-Urbani S</pubmed_authors><pubmed_authors>Garg P</pubmed_authors><pubmed_authors>Kim PM</pubmed_authors><pubmed_authors>Ivarsson Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Proteomic peptide phage display uncovers novel interactions of the PDZ1-2 supramodule of syntenin.</name><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.</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Jan</publication><modification>2026-04-07T17:12:32.797Z</modification><creation>2019-03-27T03:11:08Z</creation></dates><accession>S-EPMC4819696</accession><cross_references><pubmed>26787460</pubmed><doi>10.1002/1873-3468.12037</doi></cross_references></HashMap>