Sandbox Reserved 712: Difference between revisions
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<scene name='Sandbox_Reserved_712/P39s/1'>P39S</scene>, <scene name='Sandbox_Reserved_712/K45r/1'>K45R</scene>, M46I, <scene name='Sandbox_Reserved_712/I54v/1'>I54V</scene> and <scene name='Sandbox_Reserved_712/K55r/1'>K55R</scene> cause structural changes in the flap region and the flap hinge. | <scene name='Sandbox_Reserved_712/P39s/1'>P39S</scene>, <scene name='Sandbox_Reserved_712/K45r/1'>K45R</scene>, M46I, <scene name='Sandbox_Reserved_712/I54v/1'>I54V</scene> and <scene name='Sandbox_Reserved_712/K55r/1'>K55R</scene> cause structural changes in the flap region and the flap hinge. | ||
The pictures on the right (Fig.3 and Fig.4) show the regions (indicated in blue) that undergo structural changes caused by the mutations. | The pictures on the right (Fig.3 and Fig.4) show the regions (indicated in blue) that undergo structural changes caused by the mutations. | ||
To see the full images, with changes in PR<sub>DRV1</sub> and comparative structure of wild-type PR<sub>DRV1</sub> and PR<sub>DRV5</sub> follow the links: | To see the full images, with changes in PR<sub>DRV1</sub> and comparative structure of wild-type, PR<sub>DRV1</sub> and PR<sub>DRV5</sub> follow the links: | ||
[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2738195/figure/f4/ Structural changes in PR<sub>DRV</sub> mutants relative to wild-type PR] and | [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2738195/figure/f4/ Structural changes in PR<sub>DRV</sub> mutants relative to wild-type PR] and | ||
[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2738195/figure/f5/ Detailed view of the darunavir-enzyme interactions] | [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2738195/figure/f5/ Detailed view of the darunavir-enzyme interactions] | ||
It was discovered that the inhibitor substituents can adjust their positions depending on changes of the substrate binding pockets. Among them the P2' aminophenyl moiety undergoes the biggest changes. <ref name="Molecular" /> | It was discovered that the inhibitor substituents can adjust their positions depending on changes of the substrate binding pockets. Among them the P2' aminophenyl moiety undergoes the biggest changes. <ref name="Molecular" /> | ||
== '''Applications''' == | == '''Applications''' == | ||
