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Figure 1.
Figure 1. FXI structure. (a) Topology of the four apple
domains is represented with the protease domain removed.
Connecting loops are colored black and the loop after A4, which
leads to the C-terminal protease domain, is colored dark blue.
(b) Topology of the FXI dimer with the protease domain colored
red and Cys321 disulfide located centrally. (c) Two close-up
views of the A4 dimer interface related by a 90° rotation.
Left, interacting side chains from one side of the dimer
interface are colored yellow, making contact with a
charge-surface representation of the other half of the interface
(blue, positive; red, negative). Right, a ribbon diagram shows a
rotated view of the A4 dimer with hydrogen bonds and
electrostatic interactions colored orange.
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