Molecular architecture of mouse activating NKR-P1 receptors.

Abstract

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.

• Authors: Petr Kolenko, Daniel Rozbeský, Ondřej Vaněk, Vladimír Kopecký Jr, Kateřina Hofbauerová, Petr Novák, Petr Pompach, Jindřich Hašek, Tereza Skálová, Karel Bezouška, Jan Dohnálek
• Journal: Journal of structural biology (J Struct Biol) Vol. 175 Issue 3 Pg. 434-41 (Sep 2011) ISSN: 1095-8657 [Electronic] United States
• PMID: 21600988 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2011 Elsevier Inc. All rights reserved.

Chemical References

• NK Cell Lectin-Like Receptor Subfamily B

Topics

• Amino Acid Sequence
• Animals
• Killer Cells, Natural (metabolism)
• Mice
• Molecular Sequence Data
• NK Cell Lectin-Like Receptor Subfamily B (chemistry, metabolism)
• Protein Structure, Secondary
• Spectrum Analysis, Raman
• X-Ray Diffraction