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http://purl.uniprot.org/citations/33398170http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33398170http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33398170http://www.w3.org/2000/01/rdf-schema#comment"Proteome integrity depends on the ubiquitin-proteasome system to degrade unwanted or abnormal proteins. In addition to the N-degrons, C-terminal residues of proteins can also serve as degradation signals (C-degrons) that are recognized by specific cullin-RING ubiquitin ligases (CRLs) for proteasomal degradation. FEM1C is a CRL2 substrate receptor that targets the C-terminal arginine degron (Arg/C-degron), but the molecular mechanism of substrate recognition remains largely elusive. Here, we present crystal structures of FEM1C in complex with Arg/C-degron and show that FEM1C utilizes a semi-open binding pocket to capture the C-terminal arginine and that the extreme C-terminal arginine is the major structural determinant in recognition by FEM1C. Together with biochemical and mutagenesis studies, we provide a framework for understanding molecular recognition of the Arg/C-degron by the FEM family of proteins."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.org/dc/terms/identifier"doi:10.1038/s41589-020-00703-4"xsd:string
http://purl.uniprot.org/citations/33398170http://purl.org/dc/terms/identifier"doi:10.1038/s41589-020-00703-4"xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Mi W."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Mi W."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Song L."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Song L."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Yan X."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Yan X."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Zhou M."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Zhou M."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Dong C."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Dong C."xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Li Y.'"xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/author"Li Y.'"xsd:string
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/33398170http://purl.uniprot.org/core/date"2021"xsd:gYear