KAVAN, Daniel, Monika KUBÍČKOVÁ, Jan BILÝ, Ondřej VANĚK, Kateřina HOFBAUEROVÁ, Mrázek HYNEK, Rozbeský DANIEL, Bojarová PAVLA, Vladimír KŘEN, Lukáš ŽÍDEK, Vladimír SKLENÁŘ and Karel BEZOUŠKA. Cooperativity between subunits is essential for high affinity binding of N-acetylhexosamines to dimeric soluble and dimeric cellular forms of human CD69. Biochemistry. Washington, USA: American Chemical Society, 2010, vol. 49, No 19, p. 4060-4067. ISSN 0006-2960.
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Basic information
Original name Cooperativity between subunits is essential for high affinity binding of N-acetylhexosamines to dimeric soluble and dimeric cellular forms of human CD69
Authors KAVAN, Daniel (203 Czech Republic), Monika KUBÍČKOVÁ (203 Czech Republic, belonging to the institution), Jan BILÝ (203 Czech Republic), Ondřej VANĚK (203 Czech Republic), Kateřina HOFBAUEROVÁ (203 Czech Republic), Mrázek HYNEK (203 Czech Republic), Rozbeský DANIEL (203 Czech Republic), Bojarová PAVLA (203 Czech Republic), Vladimír KŘEN (203 Czech Republic), Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution), Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution) and Karel BEZOUŠKA (203 Czech Republic).
Edition Biochemistry, Washington, USA, American Chemical Society, 2010, 0006-2960.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 3.226
RIV identification code RIV/00216224:14310/10:00044022
Organization unit Faculty of Science
UT WoS 000277398100008
Keywords in English NMR CD69 lectin-type proteins NK cell glycoproteins
Changed by Changed by: prof. Mgr. Lukáš Žídek, Ph.D., učo 38990. Changed: 2/4/2014 12:37.
Abstract
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.
Links
LC06030, research and development projectName: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
MSM0021622413, plan (intention)Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
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