Figure 4
Figure 4. Feature and structural modeling of RHOA mutations in ATLL. (A) Representative two independent co-occurring RHOA mutations in ATLL cases. ATLL_C-05 (top) and ATLL_A-07 (bottom) cases have Gly17Arg/Gly14Val and Thr19Ile/Cys16Arg mutations, respectively. (B) Amino acid alignment of RHOA proteins from different species. Evolutionally conserved amino acids among species are shown in blue and the amino acid positions of mutation in ATLL are highlighted by arrowhead. Conserved functional domains are also indicated. (C) Mutated amino acid positions identified in ATLL are mapped to the 3D structure of the GTP-biding pocket of human RHOA protein (Protein Data Bank identification, 1A2B). GTPγS and the magnesium ion are shown as white sticks and a green sphere.

Feature and structural modeling of RHOA mutations in ATLL. (A) Representative two independent co-occurring RHOA mutations in ATLL cases. ATLL_C-05 (top) and ATLL_A-07 (bottom) cases have Gly17Arg/Gly14Val and Thr19Ile/Cys16Arg mutations, respectively. (B) Amino acid alignment of RHOA proteins from different species. Evolutionally conserved amino acids among species are shown in blue and the amino acid positions of mutation in ATLL are highlighted by arrowhead. Conserved functional domains are also indicated. (C) Mutated amino acid positions identified in ATLL are mapped to the 3D structure of the GTP-biding pocket of human RHOA protein (Protein Data Bank identification, 1A2B). GTPγS and the magnesium ion are shown as white sticks and a green sphere.

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