{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["13"],"submitter":["Zhao D"],"pubmed_abstract":["Tyrosine sulfation plays a vital role in various biochemical reactions. Although sulfated tyrosine (sTyr) has a similar structure to phosphotyrosine (pTyr), the number of available sTyr sites is significantly less than that of pTyr sites, mainly because of the lack of effective sTyr probes. A few sTyr binders were identified on the basis of structural similarity by engineering the pTyr-binding pocket of an Src Homology 2 (SH2) domain through phage selections against sTyr peptides. Nevertheless, they still interact with pTyr peptides with comparable affinity. This study aims to identify sTyr superbinders using the SH2 domain as a template. We created a distinctive phage selection scheme that separately covered selections against sTyr and pTyr peptides, followed by next-generation sequencing"],"journal":["Frontiers in microbiology"],"pagination":["901558"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9204161"],"repository":["biostudies-literature"],"pubmed_title":["Engineering of Src Homology 2 Domain Leading to Sulfotyrosine Recognition With a High Affinity by Integrating a Distinctive Selection Theme and Next-Generation Sequencing."],"pmcid":["PMC9204161"],"pubmed_authors":["Yin Y","Li C","Zhou C","Jiang H","Huang H","Qi Y","Zhao D","Li L"],"additional_accession":[]},"is_claimable":false,"name":"Engineering of Src Homology 2 Domain Leading to Sulfotyrosine Recognition With a High Affinity by Integrating a Distinctive Selection Theme and Next-Generation Sequencing.","description":"Tyrosine sulfation plays a vital role in various biochemical reactions. Although sulfated tyrosine (sTyr) has a similar structure to phosphotyrosine (pTyr), the number of available sTyr sites is significantly less than that of pTyr sites, mainly because of the lack of effective sTyr probes. A few sTyr binders were identified on the basis of structural similarity by engineering the pTyr-binding pocket of an Src Homology 2 (SH2) domain through phage selections against sTyr peptides. Nevertheless, they still interact with pTyr peptides with comparable affinity. This study aims to identify sTyr superbinders using the SH2 domain as a template. We created a distinctive phage selection scheme that separately covered selections against sTyr and pTyr peptides, followed by next-generation sequencing","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-04-07T13:21:29.906Z","creation":"2024-11-07T13:41:31.182Z"},"accession":"S-EPMC9204161","cross_references":{"pubmed":["35722314"],"doi":["10.3389/fmicb.2022.901558"]}}