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. 2007 Jun 14;26(13):3250–3259. doi: 10.1038/sj.emboj.7601744

Figure 5.

Figure 5

The binding site of the single domains on the RAS molecule. (A) A stereo diagram of the HRAS(G12V)-GTP-Fv binding interface. HRAS(G12V) is in green and the VH and VL chains are in cyan and orange, respectively. The CDRs of VH and VL are in yellow and lemon and the RAS switch I and II regions are in red and purple, respectively. Residues involved in the interface are shown in cylinder configuration. Specific residues of RAS are shown in blue, VH in red and VL in brown. Putative hydrogen bonds are indicated by dashed lines. (B) Schematic representation of the interacting residues in HRAS (green) and in the anti-RAS antibody (VH, yellow; VL, lemon). Putative hydrogen bonds are indicated by dotted lines. (C) The structures of HRAS(G12V)-GTP (green, red and purple) bound to anti-RAS Fv and of HRAS-GDP (blue) (PDB, 4Q21) (Milburn et al, 1990) are superimposed to illustrate the selectivity of iDab#6 single VH domain binding to activated GTP-bound RAS.