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The How and Why of Ca2+ Involvement in Lectin Activity

Journal

TRENDS IN GLYCOSCIENCE AND GLYCOTECHNOLOGY
Volume 23, Issue 132, Pages 168-177

Publisher

GAKUSHIN PUBL CO
DOI: 10.4052/tigg.23.168

Keywords

agglutinin; calnexin; dystroglycan; pentraxin; protein kinase; selectin

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Cell surface glycans are biochemical signals for communication with the environment. They are translated into biological responses by first binding to lectins, this recognition process thereupon triggering ensuing post-binding signaling. The specificity of this interaction must necessarily be exquisite to preclude errors. Toward this end Ca2+ is recruited to the realm of protein-carbohydrate interactions. Intriguingly, not one but different strategies how Ca2+ assists in singling out the correct sugar ligands are operative. This review dissects the different ways Ca2+ functions as an integral component of various lectins' carbohydrate-binding domains. It spans the range from the role of Ca2+ in structurally organizing the contact site without direct interaction to the ligand to interplays with charged and even neutral ligands. Finally, a case of an intricate network of up to four coordination bonds of Ca2+ with a galactose moiety is presented.

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