Introduction
Overall Structure
- Asymmetric dimer
- Consists of α-helices, β-sheets (mostly on one side of the molecule) with a heme buried inside the protein
- Two molecules of 2-hydroxypropyl-β-cyclodextrin are found near the dimer interface
Binding Interactions
-catalyzes initial step for converting vitamin D into 25-hydroxyvitamin D
-mutation causes rickets-25-hydroxylase deficiency
-has closed conformation, substrate access channel mostly covered
-secosteroid binding, extended active site
Additional Features
This molecule has a heme which is bound to iron, which, combined with its structural conformation, allows for hydroxylation with the attached substrate. This molecule carries out important functions and is not species or sex specific.
Quiz Question 1
(merely an example of what this section might look like)
rom can you identify the green, red, and blue parts of the molecule?
See Also
Credits
Introduction - Sami Kriksceonaitis
Overall Structure - Kati Johnson
Drug Binding Site - Isabel Hand
Additional Features - Elizabeth Humble
Quiz Question 1 - Matthew Tiller
References
- ↑ Strushkevich N, Usanov SA, Plotnikov AN, Jones G, Park HW. Structural analysis of CYP2R1 in complex with vitamin D3. J Mol Biol. 2008 Jun 27;380(1):95-106. Epub 2008 Apr 8. PMID:18511070 doi:10.1016/j.jmb.2008.03.065
