Sandbox Reserved 1716: Difference between revisions

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 ===Transmembrane Helices===
-The Transmembrane helices are named Transmembrane Helix 1, Transmembrane Helix 2, Transmembrane Helix 3, and Transmembrane Helix 4. The residues on Transmembrane Helix 2 (TM2) and Transmembrane Helix 4 (TM4) are significant for the binding of Vitamin K to the hydrophobic pocket of the enzyme. Asparagine 83 on TM2 and Tyrosine 142 hydrogen bond to Vitamin K Epoxide, in order to hold it in place so that it may be reduced. The angle in which Vitamin K Epoxide binds is significant to the placement of the beta hairpin, and loop 3-4. Cysteine residues from the beta hairpin and loop 3-4 will donate their electrons to Vitamin K Epoxide to open the epoxide ring, and reform Vitamin K Quinone.
+The Transmembrane region has four helices, labeled 1-4. Transmembrane Helix 2 (TM2) and 4 (TM4) contribute to the binding of Vitamin K to the hydrophobic pocket for reduction. Asparagine 83 on TM2 and Tyrosine 142 on TM4 hydrogen bond to Vitamin K Epoxide to hold it in the correct orientation for reduction. The angle in which Vitamin K Epoxide binds in the central pocket is significant to the placement of the beta hairpin, and loop 3-4, Cysteine residues C51-C132 will donate their electrons to Vitamin K Epoxide (Fig. 4) to open the epoxide ring, and reform Vitamin K Quinone (Fig. 2).
 ===Cap Domain===

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