Sandbox Reserved 431
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This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
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Vitamin D activation by cytochrome P450, rickets (3c6g)[1]
by Isabel Hand, Elizabeth Humble, Kati Johnson, Samantha Kriksceonaitis, and Matthew Tiller
Student Projects for UMass Chemistry 423 Spring 2016
Introduction
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Overall Structure
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- 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
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-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
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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)
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from 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