Number of the records: 1
Molecular architecture of mouse activating NKR-P1 receptors
- 1.
SYSNO ASEP 0363604 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Molecular architecture of mouse activating NKR-P1 receptors Author(s) Kolenko, Petr (UMCH-V) RID
Rozbeský, Daniel (MBU-M)
Vaněk, Ondřej (MBU-M)
Kopecký, V. Jr. (CZ)
Hofbauerová, Kateřina (MBU-M) ORCID
Novák, Petr (MBU-M) RID, ORCID
Pompach, Petr (MBU-M) RID, ORCID
Hašek, Jindřich (UMCH-V) RID
Skálová, Tereza (UMCH-V) RID
Bezouška, Karel (MBU-M)
Dohnálek, Jan (UMCH-V) RIDSource Title Journal of Structural Biology. - : Elsevier - ISSN 1047-8477
Roč. 175, č. 3 (2011), s. 434-441Number of pages 8 s. Language eng - English Country US - United States Keywords NK cell ; C-type lectin-like receptor ; X-ray structure Subject RIV CE - Biochemistry R&D Projects 1M0505 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA303/09/0477 GA ČR - Czech Science Foundation (CSF) GD305/09/H008 GA ČR - Czech Science Foundation (CSF) GA305/07/1073 GA ČR - Czech Science Foundation (CSF) GAP207/10/1040 GA ČR - Czech Science Foundation (CSF) KJB101120805 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z40500505 - UMCH-V (2005-2011) AV0Z50200510 - MBU-M (2005-2011) UT WOS 000293807000019 DOI 10.1016/j.jsb.2011.05.001 Annotation Receptors belonging to NKR-P1 family and their specific Clr ligands form an alternative missing self recognition system critical in immunity against tumors and viruses, elimination of tumor cells subjected to genotoxic stress, activation of T cell dependent immune response, and hypertension. The three-dimensional structure of the extracellular domain of the mouse natural killer (NK) cell receptor mNKR-P1Aex has been determined by X-ray diffraction. The core of the C-type lectin domain (CTLD) is homologous to the other CTLD receptors whereas one quarter of the domain forms an extended loop interacting tightly with a neighboring loop in the crystal. This domain swapping mechanism results in a compact interaction interface. A second dimerization interface resembles the known arrangement of other CTLD NK receptors. A functional dimeric form of the receptor is suggested, with the loop, evolutionarily conserved within this family, proposed to participate in interactions with ligands. Workplace Institute of Macromolecular Chemistry Contact Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Year of Publishing 2012
Number of the records: 1