3rs1 | pdb_00003rs1

Mouse C-type lectin-related protein Clrg

spinqualitylabelsall models 3rs1, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rs1 is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL Gene: Clec2i, Clrg, Dcl1, Ocilrp2 (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CLC2I_MOUSE] Inhibits osteoclast formation. Receptor for KLRB1F. Enhances T-cell activation. Plays a role in splenocyte activation, T-cell responses and IL-2 production. Publication Abstract from PubMed 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. Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties.,Skalova T, Kotynkova K, Duskova J, Hasek J, Kovai T, Kolenko P, Novak P, Man P, Hanc P, Vanek O, Bezouska K, Dohnalek J J Immunol. 2012 Nov 15;189(10):4881-9. doi: 10.4049/jimmunol.1200880. Epub 2012, Oct 15. PMID:23071282 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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