 | Figure 6
Nature Immunology
2, 452 - 460 (2001)
doi:10.1038/87766
Crystal structure of the human natural killer cell inhibitory receptor KIR2DL1−HLA-Cw4 complexQing R. Fan, Eric O. Long
& Don C. Wiley | | | | Figure 6. A common HLA-C binding mode for KIR2DL1 and KIR2DL2.
(a) Comparison of KIR2DL1−HLA-Cw4 (red) and KIR2DL2−HLA-Cw3 (blue) complex structures. The  12 domains of HLA-Cw4 and HLA-Cw3 in the two structures have been superimposed. The elbow angle of KIR2DL1 in complex with HLA-Cw4 is 66°, close to the 70° angle found for KIR2DL2 in complex with HLA-Cw3. (b) Comparison of the structures of free KIR2DL1 (green) and KIR2DL1 bound to HLA-Cw4 (red). The D1 domains of free and bound KIR2DL1 have been superimposed. Upon binding to HLA-Cw4, the elbow angle of KIR2DL1 increases from 55° to 66°. (c) Comparison of the structures of free KIR2DL2 (pink) and KIR2DL2 bound to HLA-Cw3 (blue). The D1 domains of free and bound KIR2DL2 have been superimposed. The elbow angles found in the free and bound states of KIR2DL2 are 71° and 70°, respectively. The figure was created using RIBBONS53.
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