Figure 3 | Scientific Reports

Figure 3

From: ALS-causing mutations in profilin-1 alter its conformational dynamics: A computational approach to explain propensity for aggregation

Figure 3

Structural consequences of the PFN1 T109M mutation. (A) Superimposed crystal structure of wild type PFN1 and a 200-ns simulation model of PFN1 T109M. Wild type PFN1, grey; T109M mutant, magenta; and PLP stick model, light blue. The overall structures are very similar. (B) Superposition of the simulated models of wild type (green) and mutant PFN1 (magenta) showing the consequences of T109M mutation on the PLP-binding site. PLP stick model, light blue. The side chains of mutated residue T109 and four other residues exhibiting large displacements (Y7, W32, H134, and Y140) at the PLP-binding site are displayed and labeled. (C) A maginified view of the changes around the site of mutation. The larger Met109 side-chain forces Trp32 side-chain to swing away to a new location (arched arrow) where it is too close (indicated by the double-headed arrow) to the original PLP binding location.

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