 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](lv5014fig4mag.jpg)
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Figure 4
Electrostatic potential surface of retroviral protease protomers. The M-PMV PR monomer (a) is shown in the same orientation and on the same scale as the HIV-1 PR protomer (b) extracted from the dimeric molecule (PDB entry 3hvp ). The complete HIV-1 PR dimer is generated by the action of a vertical dyad, which creates a second copy facing the first molecule on the right. In this view, the N- and C-termini (missing in M-PMV PR) are at the bottom and the flap loops are at the top. The active-site cavity is marked by the Asn26/Asp25 residue (ball-and-stick representation). In M-PMV PR the cavity is completely covered by the curled flap. The area of positive potential on this M-PMV PR surface is influenced by the D26N substitution, but it is of note that this mutation does not influence the tendency of the protein to fold as a monomer. The electrostatic potential (negative, red; positive, blue) was calculated in APBS (Baker et al., 2001  ). |
![[Figure 4]](lv5014fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
