Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10126859" target="_blank" >RIV/00216208:11310/12:10126859 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/12:00382839 RIV/61389013:_____/12:00382839
Result on the web
<a href="http://dx.doi.org/10.4049/jimmunol.1200880" target="_blank" >http://dx.doi.org/10.4049/jimmunol.1200880</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.4049/jimmunol.1200880" target="_blank" >10.4049/jimmunol.1200880</a>
Alternative languages
Result language
angličtina
Original language name
Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties
Original language description
Interactions between C-type lectin-like NK cell receptors and their protein ligands form one of the key recognition mechanisms of the innate immune system that is involved in the elimination of cells that have been malignantly transformed, virally infected, or stressed by chemotherapy or other factors. We determined an x-ray structure for the extracellular domain of mouse C-type lectin related (Clr) protein g, a ligand for the activation receptor NKR-P1F. Clr-g forms dimers in the crystal structure resembling those of human CD69. This newly reported structure, together with the previously determined structure of mouse receptor NKR-P1A, allowed the modeling and calculations of electrostatic profiles for other closely related receptors and ligands. Despite the high similarity among Clr-g, Clr-b, and human CD69, these molecules have fundamentally different electrostatics, with distinct polarization of Clr-g. The electrostatic profile of NKR-P1F is complementary to that of Clr-g, which sug
Czech name
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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
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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
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Immunology
ISSN
0022-1767
e-ISSN
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Volume of the periodical
189
Issue of the periodical within the volume
10
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
4881-4889
UT code for WoS article
000310710600022
EID of the result in the Scopus database
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