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http://purl.uniprot.org/citations/22252131http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22252131http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22252131http://www.w3.org/2000/01/rdf-schema#comment"Phosphotyrosine-binding domains, typified by the SH2 (Src homology 2) and PTB domains, are critical upstream components of signal transduction pathways. The E3 ubiquitin ligase Hakai targets tyrosine-phosphorylated E-cadherin via an uncharacterized domain. In this study, the crystal structure of Hakai (amino acids 106-206) revealed that it forms an atypical, zinc-coordinated homodimer by utilizing residues from the phosphotyrosine-binding domain of two Hakai monomers. Hakai dimerization allows the formation of a phosphotyrosine-binding pocket that recognizes specific phosphorylated tyrosines and flanking acidic amino acids of Src substrates, such as E-cadherin, cortactin and DOK1. NMR and mutational analysis identified the Hakai residues required for target binding within the binding pocket, now named the HYB domain. ZNF645 also possesses a HYB domain but demonstrates different target specificities. The HYB domain is structurally different from other phosphotyrosine-binding domains and is a potential drug target due to its novel structural features."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2011.496"xsd:string
http://purl.uniprot.org/citations/22252131http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2011.496"xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Li D."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Li D."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Guy G.R."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Guy G.R."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Seetharaman J."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Seetharaman J."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Sivaraman J."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Sivaraman J."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Zhou X."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Zhou X."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Yusoff P."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Yusoff P."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Ng C."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Ng C."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Lim Y.P."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Lim Y.P."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Mukherjee M."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Mukherjee M."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Sze S.K."xsd:string
http://purl.uniprot.org/citations/22252131http://purl.uniprot.org/core/author"Sze S.K."xsd:string