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Figure 1.
TR-FRET analyses of the PCSK9-LDLR interaction and its
inhibition. A, in a TR-FRET assay at neutral pH, EGF(A) and
EGF(AB) compete with the LDLR ectodomain for binding to PCSK9
with low/submicromolar IC[50] values. B, in the TR-FRET assay,
full-length WT PCSK9 and WT PCSK9ΔC are equipotent at
disrupting the interaction of labeled WT PCSK9 with labeled
LDLR, demonstrating that the C-terminal domain of PCSK9 is not
required for binding. In contrast with WT PCSK9ΔC, an
unprocessed form of PCSK9ΔC (S386A) was unable to disrupt the
interaction.
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