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Figure 1.
Fig. 1. Structure of IDO–PI complex. (A) Ribbon
representation of the overall structure of human IDO. The small
and large domains are represented by blue and green ribbons,
respectively. The helices A–S are named in the order of
appearance in the primary sequence. The connecting helices (K-L
and N) are colored in cyan. The long loop connecting the two
domains is colored in red. The heme (yellow), proximal ligand
H346 (white), and heme inhibitor 4-phynylimidazole (white) are
shown in a ball-and-stick model. The helices of the large domain
create the cavity for the heme. The connecting loop (red) and
small domain above the sixth-coordination site (heme distal
side) cover the top of cavity on the heme. (B) The four proximal
helices I, G, Q, and S run in parallel. The helices N (blue) and
K-L (cyan) connect the two domains. The connecting loop (red)
and small domain above the sixth-coordination site of the heme
cover the top of the cavity on the heme.
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