Protein Science 13: 1108–1123 (2004)
HIV-1 protease molecular dynamics of a wild-type and of the V82F/I84V mutant: Possible contributions to drug resistance and a potential new target site for drugs
Alexander L. Perryman, Jung-Hsin Lin, and J. Andrew McCammon
An incorrect version of Figure 16 ▶ appeared with this paper in print. The correct figure appears below. We apologize for any confusion this may have caused.
Figure 16.
A comparison of the most open snapshots from the wild-type’s simulation to the most closed snapshot supports that anticorrelated relationship: The solid ribbon in cyan represents the wild-type’s snapshot that displayed the second smallest value for the I50–D25 distance (cyan = 19,471 psec, value = 10.7 Å; the absolute minimum was snapshot 17,505, with a value of 10.6 Å), while the monomer on the left with a solid orange ribbon shows the semiopen conformation of the 1HHP crystal structure of the apo protease. The ribbons shown in line mode depict the local maxima for the distance between I50 and D25 from the wild-type’s simulation. These maxima were the peaks from different flap opening events. The following snapshots are displayed: 11,353 = red (I50–D25 distance was 18.1 Å = the global max.), 11,574 = magenta (17.3 Å), 8647 = blue (16.6 Å). For the corresponding maxima from the mutant’s simulation, see Fig. 11. The snapshot with the smallest distance between its flap and Asp 25 (i.e., the cyan ribbon) has the largest distance between its Ear and Cheek regions.