Fig. 3

Dynamical architecture of wild-type KIT and the D816V mutant. On top. Wild-type protein. At the bottom. Mutant protein. On the left. The communication blocks identified by COMMA are mapped onto the average conformation represented as a cartoon. The mutation site is represented by a sphere (at the bottom). The protein residues are coloured according to the block they belong to and the different blocks are labelled. See Table 1 for details on the mapping between the two proteins. In the middle. Schematic representations of the proteins depicting the communication blocks identified by COMMA and the connections between them. Each block is represented by a round and is labelled. The larger the number of residues in the block, the larger the size of the round. Overlapping blocks share some residues in common. Contacting blocks are connected by covalent bonds. The black links indicate the presence of stable non-covalent interactions between blocks. Notice that non-covalent interactions are formed between blocks that share some residues in common or contact each other, but they are not displayed for a sake of clarity. On the right. Schematic representations of the proteins depicting the results obtained from MONETA. The large round in green include all residues involved in some communication pathway. The smaller blocks in blue tones represent independent dynamic segments. The size of the round depends on the number of residues involved (same scaling as for COMMA results)