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Natural Killer Cell Activation Receptor NKp30 Oligomerization Depends on ItsN-Glycosylation

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F20%3A00533400" target="_blank" >RIV/61388971:_____/20:00533400 - isvavai.cz</a>

  • Alternative codes found

    RIV/86652036:_____/20:00533400 RIV/00216208:11310/20:10413388

  • Result on the web

    <a href="https://www.mdpi.com/2072-6694/12/7/1998" target="_blank" >https://www.mdpi.com/2072-6694/12/7/1998</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/cancers12071998" target="_blank" >10.3390/cancers12071998</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Natural Killer Cell Activation Receptor NKp30 Oligomerization Depends on ItsN-Glycosylation

  • Original language description

    NKp30 is one of the main human natural killer (NK) cell activating receptors used in directed immunotherapy. The oligomerization of the NKp30 ligand binding domain depends on the length of the C-terminal stalk region, but our structural knowledge of NKp30 oligomerization and its role in signal transduction remains limited. Moreover, ligand binding of NKp30 is affected by the presence and type ofN-glycosylation. In this study, we assessed whether NKp30 oligomerization depends on itsN-glycosylation. Our results show that NKp30 forms oligomers when expressed in HEK293S GnTI(-)cell lines with simpleN-glycans. However, NKp30 was detected only as monomers after enzymatic deglycosylation. Furthermore, we characterized the interaction between NKp30 and its best-studied cognate ligand, B7-H6, with respect to glycosylation and oligomerization, and we solved the crystal structure of this complex with glycosylated NKp30, revealing a new glycosylation-induced mode of NKp30 dimerization. Overall, this study provides new insights into the structural basis of NKp30 oligomerization and explains how the stalk region and glycosylation of NKp30 affect its ligand affinity. This furthers our understanding of the molecular mechanisms involved in NK cell activation, which is crucial for the successful design of novel NK cell-based targeted immunotherapeutics.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10606 - Microbiology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Cancers (Basel)

  • ISSN

    2072-6694

  • e-ISSN

  • Volume of the periodical

    12

  • Issue of the periodical within the volume

    7

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    24

  • Pages from-to

    1998

  • UT code for WoS article

    000554160800001

  • EID of the result in the Scopus database

    2-s2.0-85088272571