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

J 2010

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

KAVAN, Daniel; Monika KUBÍČKOVÁ; Jan BILÝ; Ondřej VANĚK; Kateřina HOFBAUEROVÁ et al.

Základní údaje

Originální název

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

Autoři

Vydání

Biochemistry, Washington, USA, American Chemical Society, 2010, 0006-2960

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 3.226

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/10:00044022

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000277398100008

Klíčová slova anglicky

NMR CD69 lectin-type proteins NK cell glycoproteins

Změněno: 2. 4. 2014 12:37, prof. Mgr. Lukáš Žídek, Ph.D.

Anotace

V originále

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.

Návaznosti

LC06030, projekt VaV

Název: Biomolekulární centrum

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

KAVAN, Daniel; Monika KUBÍČKOVÁ; Jan BILÝ; Ondřej VANĚK; Kateřina HOFBAUEROVÁ; Mrázek HYNEK; Rozbeský DANIEL; Bojarová PAVLA; Vladimír KŘEN; Lukáš ŽÍDEK; Vladimír SKLENÁŘ a 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, roč. 49, č. 19, s. 4060-4067. ISSN 0006-2960.

@article{885673,
   author = {Kavan, Daniel and Kubíčková, Monika and Bilý, Jan and Vaněk, Ondřej and Hofbauerová, Kateřina and Hynek, Mrázek and Daniel, Rozbeský and Pavla, Bojarová and Křen, Vladimír and Žídek, Lukáš and Sklenář, Vladimír and Bezouška, Karel},
   article_location = {Washington, USA},
   article_number = {19},
   keywords = {NMR CD69 lectin-type proteins NK cell glycoproteins},
   language = {eng},
   issn = {0006-2960},
   journal = {Biochemistry},
   title = {Cooperativity between subunits is essential for high affinity binding of N-acetylhexosamines to dimeric soluble and dimeric cellular forms of human CD69},
   volume = {49},
   year = {2010}
}

TY  - JOUR
ID  - 885673
AU  - Kavan, Daniel - Kubíčková, Monika - Bilý, Jan - Vaněk, Ondřej - Hofbauerová, Kateřina - Hynek, Mrázek - Daniel, Rozbeský - Pavla, Bojarová - Křen, Vladimír - Žídek, Lukáš - Sklenář, Vladimír - Bezouška, Karel
PY  - 2010
TI  - Cooperativity between subunits is essential for high affinity binding of N-acetylhexosamines to dimeric soluble and dimeric cellular forms of human CD69
JF  - Biochemistry
VL  - 49
IS  - 19
SP  - 4060-4067
EP  - 4060-4067
PB  - American Chemical Society
SN  - 00062960
KW  - NMR CD69 lectin-type proteins NK cell glycoproteins
N2  - 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.
ER  -

KAVAN, Daniel; Monika KUBÍČKOVÁ; Jan BILÝ; Ondřej VANĚK; Kateřina HOFBAUEROVÁ; Mrázek HYNEK; Rozbeský DANIEL; Bojarová PAVLA; Vladimír KŘEN; Lukáš ŽÍDEK; Vladimír SKLENÁŘ a Karel BEZOUŠKA. Cooperativity between subunits is essential for high affinity binding of N-acetylhexosamines to dimeric soluble and dimeric cellular forms of human CD69. \textit{Biochemistry}. Washington, USA: American Chemical Society, 2010, roč.~49, č.~19, s.~4060-4067. ISSN~0006-2960.

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