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Figure 2.
Fig. 2. Crystal structure of Aß-bound human ABAD. (A) A
ribbon diagram with labeled secondary structures and the L[D],
L[E], and L[F] loops. Helices are shown in green, ß
strands are shown in blue, and loops are shown in pink.
Disordered regions are shown by dotted lines. (B) Superposition
of Aß-bound human ABAD (pink) and rat ABAD in complex with
NAD (blue). The L[D] loop of 3  -hydroxysteroid
dehydrogenase (3 -HSD) (PDB code
1FJH [PDB]
) is shown in yellow. NAD is shown as a stick model with gray
for carbon atoms, red for oxygen atoms, blue for nitrogen atoms,
and yellow for phosphate atoms. The proposed Aß-binding
loop is indicated. (C) Superposition of the active sites of
Aß-bound human ABAD (pink) and rat ABAD (blue), showing
distortion of the NAD binding site and the catalytic triad S155,
K162, and Y168. Colors are the same as in (B). (D) A section of
the crystal packing interactions, showing the large solvent
channels. Each ABAD molecule is shown in a different color. The
ordered ends of the L[D] loop, residues 94 and 114, are marked
as red and blue balls, respectively, and the hypothetical loops
are shown in pink as dotted lines.
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