{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jaiprashad R"],"funding":["NIGMS NIH HHS"],"pagination":["1887"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9775153"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(12)"],"pubmed_abstract":["Intrinsically disordered proteins (IDPs) are important in both normal and disease states. Small molecules can be targeted to disordered regions, but we currently have only a limited understanding of the nature of small-molecule binding sites in IDPs. Here, we show that a minimal small-molecule binding sequence of eight contiguous residues derived from the Myc protein can be ported into a different disordered protein and recapitulate small-molecule binding activity in the new context. We also find that the residue immediately flanking the binding site can have opposing effects on small-molecule binding in the different disordered protein contexts. The results demonstrate that small-molecule binding sites can act modularly and are portable between disordered protein contexts but that residues outside of the minimal binding site can modulate binding affinity."],"journal":["Biomolecules"],"pubmed_title":["Portability of a Small-Molecule Binding Site between Disordered Proteins."],"pmcid":["PMC9775153"],"funding_grant_id":["1R15GM120698"],"pubmed_authors":["De Silva SR","Fred Lucena LM","Meyer E","Metallo SJ","Jaiprashad R"],"additional_accession":[]},"is_claimable":false,"name":"Portability of a Small-Molecule Binding Site between Disordered Proteins.","description":"Intrinsically disordered proteins (IDPs) are important in both normal and disease states. Small molecules can be targeted to disordered regions, but we currently have only a limited understanding of the nature of small-molecule binding sites in IDPs. Here, we show that a minimal small-molecule binding sequence of eight contiguous residues derived from the Myc protein can be ported into a different disordered protein and recapitulate small-molecule binding activity in the new context. We also find that the residue immediately flanking the binding site can have opposing effects on small-molecule binding in the different disordered protein contexts. The results demonstrate that small-molecule binding sites can act modularly and are portable between disordered protein contexts but that residues outside of the minimal binding site can modulate binding affinity.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-21T23:19:43.597Z","creation":"2025-04-05T19:05:11.946Z"},"accession":"S-EPMC9775153","cross_references":{"pubmed":["36551315"],"doi":["10.3390/biom12121887"]}}