Sandbox Reserved 1716: Difference between revisions
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==Step I== | ===Step I=== | ||
Step I of reforming Vitamin K Epoxide through the enzyme Vitamin K Reductase (VKOR) begins in a partially oxidized open conformation. In this state, catalytic cysteines 51 and 132 form a disulfide bond. Cysteines 43 and 135 are considered "free" because they are not bound to anything in this state. The <scene name='90/904321/I/2'>central binding pocket</scene> (highlighted in hot pink) is also empty because Vitamin K Epoxide has not bound yet. In order to get to the next step, Vitamin K epoxide will enter through the isoprenyl-chain tunnel.<ref name=”Shixuan”>PMID:33154105</ref> | Step I of reforming Vitamin K Epoxide through the enzyme Vitamin K Reductase (VKOR) begins in a partially oxidized open conformation. In this state, catalytic cysteines 51 and 132 form a disulfide bond. Cysteines 43 and 135 are considered "free" because they are not bound to anything in this state. The <scene name='90/904321/I/2'>central binding pocket</scene> (highlighted in hot pink) is also empty because Vitamin K Epoxide has not bound yet. In order to get to the next step, Vitamin K epoxide will enter through the isoprenyl-chain tunnel.<ref name=”Shixuan”>PMID:33154105</ref> | ||
==Step II== | ===Step II=== | ||
After Vitamin K Epoxide enters through the isoprenyl-chain tunnel, Asn80 on TM2 and Tyr139 on TM4 <scene name='90/904322/Tyr_asn_binding_warfarin/2'>hydrogen bond</scene>. to Vitamin K Epoxide. | After Vitamin K Epoxide enters through the isoprenyl-chain tunnel, Asn80 on TM2 and Tyr139 on TM4 <scene name='90/904322/Tyr_asn_binding_warfarin/2'>hydrogen bond</scene>. to Vitamin K Epoxide. When Vitamin K Epoxide binds, there is a shift in the bonds between the cap domain, beta hairpin, and anchor. Cys135 also forms a disulfide bond with the 3' OH group on Vitamin K Epoxide. | ||
