摘要：SummarySiglec-10 is an inhibitory I-type lectin selectively recognizing sialoglycans exposed on cell surfaces, involved in several patho-physiological processes. The key role Siglec-10 plays in the regulation of immune cell functions has made it a potential target for the development of immunotherapeutics against a broad range of diseases. However, the crystal structure of the protein has not been resolved for the time being and the atomic description of Siglec-10 interactions with complex glycans has not been previously unraveled. We present here the first insights of the molecular mechanisms regulating the interaction between Siglec-10 and naturally occurring sialoglycans. We used combined spectroscopic, computational and biophysical approaches to dissect glycans' epitope mapping and conformation upon binding in order to afford a description of the 3D complexes. Our outcomes provide a structural perspective for the rational design and development of high-affinity ligands to control the receptor functionality.Graphical AbstractDisplay OmittedHighlights•We unveiled the molecular basis of sialoglycans recognition by Siglec-10•The conformation of sialoglycans drives the interaction with the protein•Siglec-10 is able to recognize and bind complex N-glycans•Our outcomes may open the venue for the design and development of novel glycomimeticsBiochemistry; Biochemistry Methods; Structural Biology; Data Analysis in Structural Biology
