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EN
ČeštinaEnglish

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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F10%3A00044022" target="_blank" >RIV/00216224:14310/10:00044022 - isvavai.cz</a>

  • Result on the web

    —

  • DOI - Digital Object Identifier

    —

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language 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 withopening 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.

  • Czech name

    —

  • Czech description

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Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

    —

Result continuities

  • Project

    <a href="/en/project/LC06030" target="_blank" >LC06030: Biomolecular centre</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2010

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Biochemistry

  • ISSN

    0006-2960

  • e-ISSN

    —

  • Volume of the periodical

    49

  • Issue of the periodical within the volume

    19

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    8

  • Pages from-to

    —

  • UT code for WoS article

    —

  • EID of the result in the Scopus database

    —

Similar results(10)

Cooperation between Subunits Is Essential for High-Affinity Binding of N-Acetyl-D-hexosamines to Dimeric Soluble and Dimeric Cellular Forms of Human CD69Synthetic N-acetylglucosamine based fully branched tetrasaccharide, a mimetic of the endogenous ligand for CD69, activates CD69+ NK cells and killer lymphocytes upon dimerization via a hydrophilic flexible linkerBiological activities of a specific ecdysteroid dimer and of selected monomeric structural analogues in the B II bioassay.