{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["de Vink PJ"],"funding":["Dutch Research Council (NWO)"],"pagination":["8998-9002"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5575475"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["56(31)"],"pubmed_abstract":["Interactions between proteins frequently involve recognition sequences based on multivalent binding events. Dimeric 14-3-3 adapter proteins are a prominent example and typically bind partner proteins in a phosphorylation-dependent mono- or bivalent manner. Herein we describe the development of a cucurbit[8]uril (Q8)-based supramolecular system, which in conjunction with the 14-3-3 protein dimer acts as a binary and bivalent protein assembly platform. We fused the phenylalanine-glycine-glycine (FGG) tripeptide motif to the N-terminus of the 14-3-3-binding epitope of the estrogen receptor α (ERα) for selective binding to Q8. Q8-induced dimerization of the ERα epitope augmented its affinity towards 14-3-3 through a binary bivalent binding mode. The crystal structure of the Q8-induced ternary complex revealed molecular insight into the multiple supramolecular interactions between the protein, the peptide, and Q8."],"journal":["Angewandte Chemie (International ed. in English)"],"pubmed_title":["A Binary Bivalent Supramolecular Assembly Platform Based on Cucurbit[8]uril and Dimeric Adapter Protein 14-3-3."],"pmcid":["PMC5575475"],"funding_grant_id":["016.150.366","024.001.035"],"pubmed_authors":["Schrader T","Brunsveld L","de Vink PJ","Milroy LG","Ottmann C","Briels JM"],"additional_accession":[]},"is_claimable":false,"name":"A Binary Bivalent Supramolecular Assembly Platform Based on Cucurbit[8]uril and Dimeric Adapter Protein 14-3-3.","description":"Interactions between proteins frequently involve recognition sequences based on multivalent binding events. Dimeric 14-3-3 adapter proteins are a prominent example and typically bind partner proteins in a phosphorylation-dependent mono- or bivalent manner. Herein we describe the development of a cucurbit[8]uril (Q8)-based supramolecular system, which in conjunction with the 14-3-3 protein dimer acts as a binary and bivalent protein assembly platform. We fused the phenylalanine-glycine-glycine (FGG) tripeptide motif to the N-terminus of the 14-3-3-binding epitope of the estrogen receptor α (ERα) for selective binding to Q8. Q8-induced dimerization of the ERα epitope augmented its affinity towards 14-3-3 through a binary bivalent binding mode. The crystal structure of the Q8-induced ternary complex revealed molecular insight into the multiple supramolecular interactions between the protein, the peptide, and Q8.","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Jul","modification":"2026-05-04T15:41:14.743Z","creation":"2019-03-27T02:54:49Z"},"accession":"S-EPMC5575475","cross_references":{"pubmed":["28510303"],"doi":["10.1002/anie.201701807"]}}