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Figure 7
Stereoview of superposed chains of M-PMV PR subunits [magenta, monomeric form (PDB entry 3sqf, chain A); red, dimeric apo form (1M, chain B); blue, dimeric form, inhibitor complex (3MI, chain B)] together with subunits of HIV-1 PR [yellow, inhibitor complex (PDB entry 4hvp, chain A); orange, apo form (PDB entry 3hvp)]. The most prominent divergence is found within the D1 hairpin fragment, i.e. the flap. Despite a gap at the tip of the flap, the 3MI model follows the trace of HIV-1 PR, which represents the classic fold of retroviral proteases in inhibitor complexes. The 1M model is significantly different; there is a kink in the flap, formed by a 310-helix, that points it down towards the active site. The 310-helix of monomeric M-PMV PR (magenta) is also clearly visible; however, it is shifted to a different segment of the flap sequence, pointing up in this illustration. The A chain of 1MI is not shown as it is practically identical to the 3MI structure.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 75| Part 10| October 2019| Pages 904-917
https://doi.org/10.1107/S2059798319011355
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