Sandbox Reserved 1709: Difference between revisions

The <scene name='90/904314/Anchor_domain/3'> anchor domain</scene> is a key part of the VKOR structure and function that protrudes from the side of VKOR with the primary role of stabilizing the enzyme within the membrane. It sits on top of the membrane surface, as shown in figure 2, such that anchor residues can interact with the cell membrane to maintain proper proximity for VKOR activity. To accomplish this, hydrophilic residues are positioned to interact with the outer hydrophilic leaflet of the bilipid membrane, while the hydrophobic residues on the anchor have strong interactions with the inner hydrophobic leaflet of the bilipid membrane. These <scene name='90/904314/Anchor_domain/5'>polar and nonpolar interactions</scene> allow for VKOR to remain in the proper membrane arrangement and proximity for Vitamin K to bind and be activated via the cap domain and active site. The anchor also serves a role in connecting the cap domain to the rest of the membrane so that it stabilizes its covering of the central binding pocket to keep the substrate within the active site during its catalytic activation. These membrane interactions allow for VKOR to stabilize in the membrane for proper activation of Vitamin K and catalytic function of the enzyme.