Sandbox Reserved 1724: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 16: | Line 16: | ||
===Overview=== | ===Overview=== | ||
The main story of vitamin K epoxide reductase can be shown through the steps of the catalytic cycle shown on this slide. The first step of the catalytic cycle I want to highlight is the top right confirmation in which KOH is bound in the active site of VKOR. Later Emma will go into some details about the bonds that occur within VKOR that stabilize this bond, but right now the most important thing to know is that KOH exists within the closed conformation of vKOR. In the second stage the conformation of VKOR changes, the amino acid residues behave differently, but the KH substrate still exists within the closed conformation. The third step to highlight is the open conformation of VKOR. On this diagram it is shown in many different ways, first with each of our previously mentioned substrates and finally with warfarin bound (which is called a closed conformation). This is labeled a closed conformation not because the actual cap is bound to the helices like in previous steps but because warfarin is a vitamin K antagonist and prevents KOH from binding the active site of our protein. Finally VKOR can also exist in the closed conformation with warfarin because as Emma mentioned there are a lot of similarities in the interactions between KOH and warfarin with vitamin k epoxide reductase. | |||
===Catalytic Cysteines=== | ===Catalytic Cysteines=== | ||
