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Figure 5.
Fig. 5. Interaction surfaces implicated in the Prx-Grx or
Prx-Trx interaction. Electrostatic potential surfaces of the
hyPrx5 Prx domain, the hyPrx5 Grx domain, human Prx5 (PDB code
1HD2), and human Trx (PDB code 1ERU) were calculated by using
the program GRASP (27). Positive and negative charges are
represented as blue and red, respectively. a, the surface of the
hyPrx5 Prx domain. Residues involved in the Prx-Grx contact in
the hyPrx5 tetramer are labeled and surrounded by a yellow
lines. The alternative interaction surface (see "Prx-Grx
Interaction") is indicated with a green line. b, the surface of
the hyPrx5 Grx domain. Residues involved in the Prx-Grx contact
of in the hyPrx5 tetramer are labeled and surrounded by a yellow
line. c, the surface of human Prx5. Residues of human Prx5
corresponding to those participating in the Prx-Grx contact of
hyPrx5 are labeled and surrounded by a yellow line. The point of
view in the figure is the same as in a. The orientation was
determined by superposing the two structures (the hyPrx5 Prx
domain and human Prx5). Thr-48, Ser-51, Phe-150, Asp-154, and
Asp-156 of the hyPrx5 Prx domain correspond to Gly-46, Lys-49,
Leu-149, Leu-153, and Pro-155 of human Prx5, respectively (for
the sequence alignment, see Fig. 2). d, the surface of human
Trx. Residues of human Trx involved in the Trx-Trx reductase
contact (PDB code 1F6M) are labeled and surrounded by a yellow
line. The point of view in the figure is the same as in b. The
orientation was determined by superposing the two structures
(the hyPrx5 Grx domain and human Trx). The C  trace of
the NF  B peptide
bound to human Trx (Ref. 38, PDB code 1MDI) was drawn as a cyan
tube.
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