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Figure 6.
FIG. 6. Alignments of side chain mutations on BCL-X[L](
 C)
structure (1BXL [PDB]
) used as docking target for AA[1]. a, alignments of BCL-X[L](
C)
structure in free (green) and BAK-BH3-bound (black)
conformations. The modeled AA[1] (light green) is shown in place
of BAK-BH3 in binding pocket. The C  RMSD for residues
Glu-92, Phe-97, Ala-142, and Phe-146 is 1.3 Å, whereas
overall C RMSD is 2.5 Å.
b-d, modeling of mutations into hydrophobic groove of 1BXL [PDB]
. Yellow stars indicate clashing contacts. b, F97W (purple)
makes two moderate clashing contacts, each at 2.6 Å. c,
the A142L mutation (magenta) makes an extreme clashing contact
with CD1 to O8 of AA[1] at 1.2 Å. d, although Phe-146
makes two van der Waals contacts with the C27 of AA[1] the F146L
mutation (orange) only makes one contact from CD1 (3.4 Å).
Nitrogen atoms are colored blue, and oxygen atoms are colored
red.
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