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. 2005 May 13;102(21):7641–7646. doi: 10.1073/pnas.0502439102

Fig. 7.

Fig. 7.

The assembly process that leads to the formation of a hexameric NKG2D–DAP10 receptor complex. (A) The data demonstrate that each TM domain of human NKG2D assembles with one DAP10 dimer and that this interaction involves both TM aspartic acids of DAP10 (red circles) and the TM arginine (blue circles). (B and C) The arrangement of the TM domains in the hexameric NKG2D–DAP10 structure (B) thus shows similarities to an assembly intermediate of the TCR–CD3 complex (C) that lacks the ζ–ζ dimer.