Publication details

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


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

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.
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