Additional file 3: Figure S1. of Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance

The relative abundances of amino acids between −10 and +10 positions of the phosphorylated or non-phosphorylated His/Asp (PDF 377 kb)

Additional file 2: Table S1. of Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance

Phospho probabilities, process method, leading protein identifier, UniProt No. (if available), protein description, and protein functional class of the identified phosphopeptides (PDF 539 kb)

Additional file 1: of Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance

MS/MS Spectra. Spectra of the identified phosphopeptides (PDF 4714 kb)

A Multivalent Marine Lectin from <i>Crenomytilus grayanus</i> Possesses Anti-cancer Activity through Recognizing Globotriose Gb3

In this study, we report the structure and function of a lectin from the sea mollusk <i>Crenomytilus grayanus</i> collected from the sublittoral zone of Peter the Great Bay of the Sea of Japan. The crystal structure of <i>C. grayanus</i> lectin (CGL) was solved to a resolution of 1.08 Å, revealing a β-trefoil fold that dimerizes into a dumbbell-shaped quaternary structure. Analysis of the crystal CGL structures bound to galactose, galactosamine, and globotriose Gb3 indicated that each CGL can bind three ligands through a carbohydrate-binding motif involving an extensive histidine- and water-mediated hydrogen bond network. CGL binding to Gb3 is further enhanced by additional side-chain-mediated hydrogen bonds in each of the three ligand-binding sites. NMR titrations revealed that the three binding sites have distinct microscopic affinities toward galactose and galactosamine. Cell viability assays showed that CGL recognizes Gb3 on the surface of breast cancer cells, leading to cell death. Our findings suggest the use of this lectin in cancer diagnosis and treatment