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Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10296025" target="_blank" >RIV/00216208:11310/15:10296025 - isvavai.cz</a>

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=5-YAbiIhHS" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=5-YAbiIhHS</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1107/S1399004714027928" target="_blank" >10.1107/S1399004714027928</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states

  • Original language description

    Human LLT1 is a C-type lectin-like ligand of NKR-P1 (CD161, gene KLRB1), a C-type lectin-like receptor of natural killer cells. Using X-ray diffraction, the first experimental structures of human LLT1 were determined. Four structures of LLT1 under various conditions were determined: monomeric, dimeric deglycosylated after the first N-acetylglucosamine unit in two forms and hexameric with homogeneous GlcNAc(2)Man(5) glycosylation. The dimeric form follows the classical dimerization mode of human CD69. The monomeric form keeps the same fold with the exception of the position of an outer part of the long loop region. The hexamer of glycosylated LLT1 consists of three classical dimers. The hexameric packing may indicate a possible mode of interaction of C-type lectin-like proteins in the glycosylated form.

  • 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

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

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

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Acta Crystallographica. Section D: Structural Biology

  • ISSN

    2059-7983

  • e-ISSN

  • Volume of the periodical

    71

  • Issue of the periodical within the volume

    March 2015

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    14

  • Pages from-to

    578-591

  • UT code for WoS article

    000351155400016

  • EID of the result in the Scopus database

    2-s2.0-84924758043