Sandbox Reserved 1709

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page George G. Papadeas/Sandbox VKOR. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Introduction Function and Biological Role Structural Highlights Active Site The active site plays a vital role in binding of any substrate or ligand to the VKOR. Upon binding, the VKOR will transition into a closed conformation that will allow its catalytic mechanism to commence. Cap Domain VKOR Cap Domain Closed conformation Disulfide Bridge Stabilization Anchor Anchor Domain Function: Method of Coagulation Brief Overview The open conformation will be prepped and waiting for a substrate or ligand to bind. Catalytic Mechanism The catalytic mechanism of VKOR is a critical part of its overall function in the body. Highly regulated enzymatic activity through the reactivity of catalytic cysteines allows VKOR to properly activate Vitamin K for its use in the body. The enzyme begins in stage 1, where it's in the open conformation with the cap domain open to allow in a substrate to bind to the active site. Once a substrate binds, the cap domain is initiated into the closed conformation. VKOR is now in stage 2. To further stabilize the closed conformation with the substrate bound, the cap domain helps initiate a catalytic reaction of cysteines to break the disulfide bridge that was stabilizing stage 1. Free cysteines are now available that provide strong stabilization of the closed conformation through interactions with the cap domain and the bound substrate. This puts the enzyme in Stage 3, where the catalytic free cysteines react to form a new disulfide bridge, releasing the activated substrate into the blood stream to promote anticoagulation. With two stable disulfide bridges and VKOR unbound, the enzyme is now in its final, unreactive Stage 4. VKOR must undergo conformational changes to return to Stage 1 and restart the catalytic process to activate Vitamin K again. Disease and Treatment Mutations Some key mutations that can be detrimental to the VKOR structure are mutations of the active site. The two main residues, N80 and Y139, can be mutated to A80 and F139 creating a decrease in recognition and stabilization This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.