3RS1

Mouse C-type lectin-related protein Clrg

Summary for 3RS1

• Entry DOI: 10.2210/pdb3rs1/pdb
• Descriptor: C-type lectin domain family 2 member I, CHLORIDE ION (3 entities in total)
• Functional Keywords: c-type lectin-like, ligand of nk receptor, natural killer cell receptors, surface of activated t lymphocytes, immune system
• Biological source: Mus musculus (mouse)
• Cellular location: Cell membrane; Single-pass type II membrane protein (By similarity): Q9WVF9
• Total number of polymer chains: 2
• Total formula weight: 28889.85

Authors

Skalova, T.,Dohnalek, J.,Duskova, J.,Stepankova, A.,Koval, T.,Hasek, J.,Kotynkova, K.,Vanek, O.,Bezouska, K. (deposition date: 2011-05-02, release date: 2012-05-02, Last modification date: 2024-11-06)

Primary citation

Skalova, T.,Kotynkova, K.,Duskova, J.,Hasek, J.,Kovai, T.,Kolenko, P.,Novak, P.,Man, P.,Hanc, P.,Vanek, O.,Bezouska, K.,Dohnalek, J.
Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties.
J.Immunol., 189:4881-4889, 2012

PubMed Abstract: 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 suggests a plausible interaction mechanism based on contacts between surface sites of opposite potential.

PubMed: 23071282
DOI: 10.4049/jimmunol.1200880

Experimental method

X-RAY DIFFRACTION (1.94 Å)