3M9Z

Crystal Structure of extracellular domain of mouse NKR-P1A

Summary for 3M9Z

• Entry DOI: 10.2210/pdb3m9z/pdb
• Related: 1E87 1EGG 1IXX
• Descriptor: Killer cell lectin-like receptor subfamily B member 1A, PHOSPHATE ION (3 entities in total)
• Functional Keywords: c-type lectin-like domain, domain swapping, disulfide bond, receptor, transmembrane protein, natural killer cell receptor, signaling protein
• Biological source: Mus musculus (mouse)
• Cellular location: Membrane; Single-pass type II membrane protein: P27811
• Total number of polymer chains: 1
• Total formula weight: 16103.74

Authors

Kolenko, P.,Rozbesky, D.,Bezouska, K.,Hasek, J.,Dohnalek, J. (deposition date: 2010-03-23, release date: 2011-04-06, Last modification date: 2024-11-27)

Primary citation

Kolenko, P.,Rozbesky, D.,Vanek, O.,Kopecky, V.,Hofbauerova, K.,Novak, P.,Pompach, P.,Hasek, J.,Skalova, T.,Bezouska, K.,Dohnalek, J.
Molecular architecture of mouse activating NKR-P1 receptors.
J.Struct.Biol., 175:434-441, 2011

PubMed 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.

PubMed: 21600988
DOI: 10.1016/j.jsb.2011.05.001

Experimental method

X-RAY DIFFRACTION (1.7 Å)