|
Figure 5.
FIG. 5. Location and structural effects of APECED causing
mutations. 1H-1D spectra (amide region) of pathological mutants
of AIRE1-PHD1 and of wild-type AIRE1-PHD1 and AIRE1-PHD2. A,
mutant C311Y; B, AIRE1-PHD1 wild type upon addition of 20 mM
EDTA; C, mutant P326Q; D, mutant P326L; asterisks indicate the
presence of additional conformers, possibly coming from a
cis-trans isomerization of P325; E, mutant V301M; F, wild-type
AIRE1 PHD1, and G, wild-type AIRE1-PHD2; H, ribbon
representation of the AIRE1-PHD1 structure (blue) and mapping of
pathological point mutations by showing their side chains in
red; the zinc-binding residues are in cyan, the cis-proline
Pro325 in yellow, and the zinc ions in pink. I, space-filled
representation of AIRE1-PHD1, with pathological mutation sites
in red, Pro325 in yellow and zinc ions in pink. Val301 and
Pro326 are partially exposed to the surface.
|
