Cooperativity between subunits is essential for high affinity binding of N-acetylhexosamines to dimeric soluble and dimeric cellular forms of human CD69

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Authors	KAVAN Daniel KUBÍČKOVÁ Monika BILÝ Jan VANĚK Ondřej HOFBAUEROVÁ Kateřina HYNEK Mrázek DANIEL Rozbeský PAVLA Bojarová KŘEN Vladimír ŽÍDEK Lukáš SKLENÁŘ Vladimír BEZOUŠKA Karel
Year of publication	2010
Type	Article in Periodical
Magazine / Source	Biochemistry
MU Faculty or unit	Faculty of Science
Citation
Field	Biochemistry
Keywords	NMR CD69 lectin-type proteins NK cell glycoproteins
Description	Binding of GlcNAc to dimeric human CD69 was followed by equilibrium dialysis, fluorescence titration, and NMR. Clear cooperativity in high affinity binding to two subunits was observed (Hill coefficient 1.94), and binding of the ligand was connected with opening of dimer structure. However, monomeric CD69 obtained by mutating Q93 and R134 at dimer interface showed much lower affinity and no cooperativity (Hill coefficient 1.07). Perturbation of dimer interface resulted in severe impairment of the signaling ability of cellular CD69 cross-linked with antibodies or a bivalent high affinity N-acetylhexosamine-based ligand.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Biomolecular centre