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Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F19%3A00505686" target="_blank" >RIV/61388955:_____/19:00505686 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/19:00505686

  • Result on the web

    <a href="https://www.mdpi.com/1422-0067/20/8/1884" target="_blank" >https://www.mdpi.com/1422-0067/20/8/1884</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/ijms20081884" target="_blank" >10.3390/ijms20081884</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Oligomeric Architecture of Mouse Activating Nkrp1 Receptors on Living Cells

  • Original language description

    Mouse activating Nkrp1 proteins are commonly described as type II transmembrane receptors with disulfide-linked homodimeric structure. Their function and the manner in which Nkrp1 proteins of mouse strain (C57BL/6) oligomerize are still poorly understood. To assess the oligomerization state of Nkrp1 proteins, mouse activating EGFP-Nkrp1s were expressed in mammalian lymphoid cells and their oligomerization evaluated by Forster resonance energy transfer (FRET). Alternatively, Nkrp1s oligomers were detected by Western blotting to specify the ratio between monomeric and dimeric forms. We also performed structural characterization of recombinant ectodomains of activating Nkrp1 receptors. Nkrp1 isoforms c1, c2 and f were expressed prevalently as homodimers, whereas the Nkrp1a displays larger proportion of monomers on the cell surface. Cysteine-to-serine mutants revealed the importance of all stalk cysteines for protein dimerization in living cells with a major influence of cysteine at position 74 in two Nkrp1 protein isoforms. Our results represent a new insight into the oligomerization of Nkrp1 receptors on lymphoid cells, which will help to determine their function.

  • 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

    10403 - Physical chemistry

Result continuities

  • Project

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

  • Continuities

Others

  • Publication year

    2019

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    International Journal of Molecular Sciences

  • ISSN

    1422-0067

  • e-ISSN

  • Volume of the periodical

    20

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    24

  • Pages from-to

    1884

  • UT code for WoS article

    000467648700082

  • EID of the result in the Scopus database

    2-s2.0-85065116228