1EFX

STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3

Summary for 1EFX

• Entry DOI: 10.2210/pdb1efx/pdb
• Related: 2dl2
• Descriptor: HLA-CW3 (HEAVY CHAIN), BETA-2-MICROGLOBULIN, PEPTIDE FROM IMPORTIN ALPHA-2, ... (5 entities in total)
• Functional Keywords: mhc, hla, class i, kir, nk cell receptor, immunoglobulin fold, receptor-mhc complex, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P61769; Cytoplasm: P52292; Cell membrane; Single-pass type I membrane protein: P43627
• Total number of polymer chains: 5
• Total formula weight: 89034.14

Authors

Boyington, J.C.,Motyka, S.A.,Schuck, P.,Brooks, A.G.,Sun, P.D. (deposition date: 2000-02-10, release date: 2000-06-14, Last modification date: 2024-11-13)

Primary citation

Boyington, J.C.,Motyka, S.A.,Schuck, P.,Brooks, A.G.,Sun, P.D.
Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand.
Nature, 405:537-543, 2000

PubMed Abstract: Target cell lysis is regulated by natural killer (NK) cell receptors that recognize class I MHC molecules. Here we report the crystal structure of the human immunoglobulin-like NK cell receptor KIR2DL2 in complex with its class I ligand HLA-Cw3 and peptide. KIR binds in a nearly orthogonal orientation across the alpha1 and alpha2 helices of Cw3 and directly contacts positions 7 and 8 of the peptide. No significant conformational changes in KIR occur on complex formation. The receptor footprint on HLA overlaps with but is distinct from that of the T-cell receptor. Charge complementarity dominates the KIR/HLA interface and mutations that disrupt interface salt bridges substantially diminish binding. Most contacts in the complex are between KIR and conserved HLA-C residues, but a hydrogen bond between Lys 44 of KIR2DL2 and Asn 80 of Cw3 confers the allotype specificity. KIR contact requires position 8 of the peptide to be a residue smaller than valine. A second KIR/HLA interface produced an ordered receptor-ligand aggregation in the crystal which may resemble receptor clustering during immune synapse formation.

PubMed: 10850706
DOI: 10.1038/35014520

Experimental method

X-RAY DIFFRACTION (3 Å)