Sandbox Reserved 1724: Difference between revisions

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==Vitamin K Epoxide Reductase==
==Vitamin K Epoxide Reductase==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.


== Introduction ==
== Introduction ==
Vitamin K epoxide reductase (VKOR) is the enzyme responsible for regenerating vitamin K from vitamin K epoxide to support blood coagulation.


=== Vitamin K Cycle ===
=== Vitamin K Cycle ===
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===Tyrosine 138 and Asparagine 80===
===Catalytic Amino Acids===
 
VKOR uses two catalytic amino acids, tyrosine 139 and asparagine 80, to stabilize vitamin K in all forms and vitamin K antagonists, such as warfarin, in the binding pocket. Tyr139 and Asn80 hydrogen bond to carbonyl groups on both structures and stabilizes them within the binding pocket.


===Hydrophobic Interactions===
===Hydrophobic Interactions===
Other than the two previously mentioned hydrogen bonds (Tyr139 and Asn80), vitamin K and antagonists are bound in via hydrophobic interactions within the binding pocket of VKOR. Hydrophobic residues of VKOR such as Phe80, Phe87, and Tyr88, form a hydrophobic tunnel within the binding pocket.


== Medical Relevance ==
== Medical Relevance ==