@article{open2611,
          volume = {532},
          number = {1},
           month = {October},
          author = {Shailza Sharma and Sonal Mahajan and Sonali Sunsunwal and Aasawari Khairnar and T N C Ramya},
            note = {Copyright of this article belongs to Elsevier Science.},
           title = {Amino acid residues important for D-galactose recognition by the F-type lectin, Ranaspumin-4.},
       publisher = {Elsevier Science/Academic Press},
            year = {2020},
         journal = {Biochemical and biophysical research communications},
           pages = {54--59},
        keywords = {F-type lectin domain; L-fucose; D-galactose; Ranaspumin-4; Site-directed mutagenesis},
             url = {http://crdd.osdd.net/open/2611/},
        abstract = {F-type lectins are typically L-fucose binding proteins with characteristic L-fucose-binding and calciumbinding sequence motifs, and an F-type lectin fold. An exception is Ranaspumin-4, an F-type lectin of the Tungra frog, Engystomops pustulosus. Ranaspumin-4 is D-galactose specific and does not bind to L-fucose although it has the conserved L-fucose binding sequence motif and shares overall sequence similarity with other F-type lectins. Here, we report the detailed glycan-binding profile of wild-type Ranaspumin-4 using hemagglutination inhibition assays, flow cytometry assays and enzyme-linked lectin assays, and identify residues important for D-galactose recognition using rational site-directed mutagenesis. We demonstrate that Ranaspumin-4 binds to terminal D-galactose in alpha or beta linkage with preference for alpha 1-3, alpha 1-4,beta 1-3, and beta 1-4 linkages. Further, we find that a methionine residue (M31) in Ranaspumin-4 that occurs in place of a conserved Gln residue (in other F-type lectins), supports D-galactose recognition. Resides Q42 and F156 also likely aid in D-galactose recognition. (C) 2020 Elsevier Inc. All rights reserved.}
}