1M4K

Crystal structure of the human natural killer cell activator receptor KIR2DS2 (CD158j)

Summary for 1M4K

• Entry DOI: 10.2210/pdb1m4k/pdb
• Descriptor: KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 2DS2, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: beta-sandwich, ig-like c2 type domain, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Single-pass type I membrane protein: P43631
• Total number of polymer chains: 1
• Total formula weight: 22206.73

Authors

Saulquin, X.,Gastinel, L.N.,Vivier, E. (deposition date: 2002-07-03, release date: 2003-04-15, Last modification date: 2024-11-20)

Primary citation

Saulquin, X.,Gastinel, L.N.,Vivier, E.
Crystal structure of the human natural killer cell activating receptor KIR2DS2 (CD158j)
J.EXP.MED., 197:933-938, 2003

PubMed Abstract: Killer cell Ig-like receptors (KIRs) regulate the function of human natural killer and T cell subsets. A feature of the KIR locus is the clustering of homologous genes encoding for inhibitory and activating KIR. Inhibitory and activating KIR differ for ligand specificities and/or affinities. In particular, we show here with KIR tetramers that activating KIR2DS2 does not bind HLA-Cw3 molecules recognized by inhibitory KIR2DL2, despite 99% extracellular amino acid identity. We also report the 2.3-A structure of KIR2DS2, which reveals subtle displacements of two residues (Tyr45 and Gln71) involved in the interaction of KIR2DL2 with HLA-Cw3. These results show that KIR molecules cannot tolerate any variability in their three-dimensional structure without altering their MHC class I recognition capacities. Therefore, the mode of recognition used by KIR largely differs from the conformational changes that characterize T cell receptor or NKG2D interaction with their respective ligands.

PubMed: 12668644
DOI: 10.1084/jem.20021624

Experimental method

X-RAY DIFFRACTION (2.3 Å)