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Figure 2.
FIG. 2. Local structure at the site of Phe-508 in NBD1 of
CFTR. A, stereo image of conformation of Phe-508 loop region in
mNBD1 (gold), hNBD1-2b-F508A (cyan), and hNBD1-7a-  F508
(blue). B and C, worm diagrams of hNBD1-2b-F508A (B) and
hNBD1-7a- F508 (C). Residues
507-510 in B are modeled from the mNBD1 structure. The position
of Phe-508 is shown in green. Positions of residues 507 and 509
are shown in gold. Helices in are red,  -strands are in blue. D
and E, surface properties of hNBD1-2b-F508A (D) and hNBD1-7a-
F508 (E) in same
orientations as in B and C. Residues 507-510 in hNBD1-2b-F508A
structure have been replaced with those from the mNBD1 structure
to provide an image representative of the wild-type human
protein. Residues are colored to indicate hydrophobic (green),
negatively charged (red), positively charge (blue), and neutral
(white) side chains. The "F " label indicates the side chain of
Phe-508, and "V " indicates the side chain of Val-510. White
worms indicate the position of the L-loop from BtuCD (residues
217-227 from PDB id 117v:A) after least squares alignment of the
ABC  subdomain from its NBD
with that from hNBD1. The structural differences visible at the
right side of these images derives from a change in the
conformation of the helix 4C-helix 5 loop and is likely a
results of variation in packing contacts between the two crystal
structures. The figure was made using Spock (31).
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