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Figure 3.
Structure of insulin-bound IDE. A, global view of the
structure of insulin-bound IDE-CF-E111Q monomer. IDE domains
1–4 (IDE-D1 to IDE-D4) are colored green, blue, yellow, and
red, respectively. Insulin A and B chains are colored magenta
and cyan, respectively. The zinc ion is colored gray. B,
composite omit map of insulin contoured at 1.5σ. C,
electrostatic surface representation of insulin and IDE. The
molecular surface is color-coded as calculated by Adaptive
Poisson-Boltzmann Solver. The molecular surface is colored as
calculated by Adaptive Poisson-Boltzmann Solver (51) (<–6 kT
in red, 0 kT in white, and >+6 kT in blue). The interaction
surface between the N- and C-terminal domains of IDE and insulin
is marked by yellow dashed lines based on the contact residues
displayed using CCP4 molecular graphics (30).
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