Cooperation between subunits is essential for high-affinity binding of N-acetyl-D-hexosamines to dimeric soluble and dimeric cellular forms of human CD69

0350684 - MBÚ 2011 RIV US eng J - Journal Article
Kavan, Daniel - Kubíčková, M. - Bílý, J. - Vaněk, O. - Hofbauerová, Kateřina - Mrázek, H. - Rozbeský, Daniel - Bojarová, Pavla - Křen, Vladimír - Žídek, L. - Sklenář, V. - Bezouška, K.
Cooperation between subunits is essential for high-affinity binding of N-acetyl-D-hexosamines to dimeric soluble and dimeric cellular forms of human CD69.
Biochemistry. Roč. 49, č. 19 (2010), s. 4060-4067. ISSN 0006-2960
R&D Projects: GA MŠMT 1M0505; GA ČR GA303/09/0477; GA ČR GD305/09/H008; GA ČR GP203/09/P024
Institutional research plan: CEZ:AV0Z50200510
Keywords : cd 69 * N-acetyl-D-hexosamines * lymphocyte
Subject RIV: CE - Biochemistry
Impact factor: 3.226, year: 2010

CD69 is an earliest lymphocyte activation antigen and a universal leukocyte triggering molecule expressed at sites of active immune response. The binding of GlcNAc to the dimeric human CD69 was followed by equilibrium dialysis, fluorescence titration, and NMR. Clear cooperation was observed in the high-affinity binding (K(d) = 4.0 x 10(-7) M) of the carbohydrate to two subunits of the dimeric CD69 (Hill coefficient 1.94). A control monosaccharide ManNAc was not bound by human CD69, and both monosaccharides had no effects on the structure of the receptor
Permanent Link: http://hdl.handle.net/11104/0190621