Structural Determinants of Misfolding in Multidomain Proteins
Fig 3
Folded and misfolded topologies of Src SH3.
(a) Schematic of Src SH3 fold, in which the three-dimensional β sheet structure (shown in (b)) is unrolled into two dimensions, for each domain (N-terminal and C-terminal in blue and red respectively). On the N-terminal domain are indicated the sequence positions K ∈ {0, 18, 37, 46} characterizing the possible circularly permuted “central domains”, with K = 0 corresponding to the native fold and K > 0 indicating the approximate starting residue for the “central domain” misfold. (c), (e), (g): two dimensional representations of the observed misfolded topologies of Src SH3. In each case, the residue K characterizing the misfold is indicated by the bullet point and the central domain is enclosed by a broken rectangle. (d), (f), (h): three-dimensional representations of the misfolds shown in (c),(e),(g) respectively.