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Figure 4.
Fig. 4. The predicted interaction of A20 with ubiquitin. (a
and b) Mapping of conserved residues on the A20 surface. The
location of the active site is circled. (c) Ribbon diagram of
A20 with modeled ubiquitins. The locations of the ubiquitin
based on the HAUSP–ubiquitin and Yuh1–ubiquitin complexes
are shown in gray and orange, respectively. The location of the
ubiquitin after adjustment to avoid steric clash is shown in
yellow. (d) Surface presentation of A20 shown in complex with
the modeled ubiquitin in a ribbon diagram. The active site is
circled. (e) Electrostatic surface presentation of A20 shown in
complex with the modeled ubiquitin in a ribbon diagram. The
ubiquitin-binding site is mostly negatively charged. (f and g)
The model of the A20–ubiquitin complex shown with A20 in a
ribbon diagram and the ubiquitin in an electrostatic surface
representation. The positive electrostatic potential of the side
of ubiquitin in contact with A20 is shown. (h) The proposed
oxyanion hole construction of A20 by the main-chain amides of
Cys103, Gly101, and Asp100. The corresponding regions in Yuh1
and HAUSP are superimposed and shown.
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