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Figure 1.
FIG. 1. Crystal structure of Fc  RI ectodomain. a,
stereo ribbon drawing of the structure of Fc RI. EC1 is the
N-terminal domain, and EC2 is the C-terminal domain. Disulfide
bonds are shown in green. The residues 56-59 and 196-199 were
disordered in the electron density map. b, topological diagram
of the ectodomain of Fc RI. The arrows show the
directions of  -strands, whereas the
3[10] helix structures are represented by two circles. The amino
acid residues at each end of -strands and helices are
numbered. c, close-up stereo view of the hydrophobic core in the
interdomain interface of Fc RI. The 12 residues
responsible for stabilizing the hydrophobic core are shown in
ball-and-stick representation. Tyr173 (Y173) is colored yellow,
Tyr181 (Y181) blue, and Trp183 (W183) green. Other residues are
colored using the CPK (Corey-Pauling-Kendrew) convention (blue,
nitrogen; red, oxygen; gray, carbon; yellow, sulfur) color
scheme.
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