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Figure 5.
Figure 5. The Empty Cavity in the Dimer Interface of LOX-1
(A) Empty cavity located at the dimer interface in the
LOX-1 disulfide-lined dimer structure. The surrounding residues
of the cavity are shown as bold lines.
(B) Possible effect
of the W150A mutation on the basic spine structure on the LOX-1
ligand recognition surface. The W150A mutation may resize the
empty cavity in the dimer interface, which subsequently
disarranges the dimer, resulting in the disruption of the basic
spine structure. The disrupted basic spine structure should lead
to severe reduction of the binding ability to ligands.
(C)
A plausible representation of the entire structure of LOX-1 at
the cell surface, based on the crystal structure for CTLD and
the model structure for the NECK. Modeling was performed by
using the myosin heavy chain coiled-coil structure, which shows
a high level of sequence homology to the NECK region.
(D)
Scale comparison between the the OxLDL particle and LOX-1 dimer.
The assembled structure of LOX-1 is drawn according to the
results of cell biology studies that showed LOX-1 to exist as a
hexamer on the cell surface (Xie et al., 2004). The diameter of
OxLDL was estimated from cryoelectron microscopic observation of
the LDL particle (Segrest et al., 2001). In this comparison, it
is assumed that no significant structural alterations are
induced by oxidation to the LDL particle.
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