Sandbox Reserved 1709: Difference between revisions

Structural characterization of VKOR has been difficult due to its in vitro instability. Recently, a series of atomic structures have been determined utilizing anticoagulant stabilization and VKOR-like [https://pubmed.ncbi.nlm.nih.gov/33154105/ homologs]. Crystal structures of VKOR were captured with a bound substrate (KO) or vitamin K antagonist (VKA) (PDB Codes: Table 1)<ref>DOI 10.1126</ref>. VKA substrates utilized were anticoagulants, namely [https://en.wikipedia.org/wiki/Warfarin Warfarin], [https://en.wikipedia.org/wiki/Brodifacoum Brodifacoum], [https://en.wikipedia.org/wiki/Phenindione Phenindione], and [https://en.wikipedia.org/wiki/Chlorophacinone Chlorophacinone]. Second, VKOR-like homologs were utilized to aid in structure classification. Homologs refer to specific cysteine residues that have been mutated to serine to facilitate capturing a stable conformation state. Homologs were mainly isolated from human VKOR with some isolated from the pufferfish ''Takifugu rubripes''. Furthermore, all of the structures used have been processed to remove a beta barrel at the south end of VKOR that served no purpose in function of the enzyme. This also allowed for the residue numbering to be reassigned and more closely replicate the human VKOR.