Figure 3
Figure 3. Modeling of FTase β mutations onto the lonafarnib/FPTase cocrystal structure. (A, left) Four of the mutated residues found are on the molecular surface of the active site (C95R, W106R, P152S, and Y361H,L,S; surfaces of the corresponding amino acid side chains are denoted in yellow). (A, right) Mapping of all the residues for which mutations were identified. Purple indicates residues that are not directly on the surface of the active site. (B) Close-up view of the residues identified. (C) A close-up view of residues in close proximity with lonafarnib (W106, Y361, and C95). Black lines mark distances of less than 4 Å.

Modeling of FTase β mutations onto the lonafarnib/FPTase cocrystal structure. (A, left) Four of the mutated residues found are on the molecular surface of the active site (C95R, W106R, P152S, and Y361H,L,S; surfaces of the corresponding amino acid side chains are denoted in yellow). (A, right) Mapping of all the residues for which mutations were identified. Purple indicates residues that are not directly on the surface of the active site. (B) Close-up view of the residues identified. (C) A close-up view of residues in close proximity with lonafarnib (W106, Y361, and C95). Black lines mark distances of less than 4 Å.

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