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- W2885402856 abstract "Discerning the different interaction states during dynamic protein-ligand binding is difficult. Here we apply site-specific cysteine-α-chloroacetyl cross-linking to scrutinize the binding between the Src homology 2 (SH2) domain and phosphotyrosine (pY) peptides, a highly dynamic interaction that is a key to cellular signal transduction. From a model SH2 protein to a set of representative SH2 domains, we showed here that a proximity-induced cysteine-α-chloroacetyl reaction cross-linked two spatially adjacent chemical groups as a result of the binding interaction, and reciprocally, the information about the interaction states can be deduced from the cross-linked products. To our surprise, we found SH2 domains can adopt a reverse binding mode with single-pronged, two-pronged, and half pY peptides. This finding was further supported by a set of 500 ns molecular dynamics simulations. This serendipitous finding defies the canonical theory of SH2 binding, suggests a possible answer about the source of the versatility of SH2 signaling, and sets a model for other protein binding interactions." @default.
- W2885402856 created "2018-08-22" @default.
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- W2885402856 date "2018-08-09" @default.
- W2885402856 modified "2023-10-17" @default.
- W2885402856 title "Reverse Binding Mode of Phosphotyrosine Peptides with SH2 Protein" @default.
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- W2885402856 doi "https://doi.org/10.1021/acs.biochem.8b00677" @default.
- W2885402856 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30091902" @default.
- W2885402856 hasPublicationYear "2018" @default.
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