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==Introduction== | ==Introduction== | ||
Rickets is a disease caused by a vitamin D deficiency. Vitamin D can be obtained from ultra violet radiation and from various food sources. Cytochrome P450 enzymes are involved in the first step to regulate and process vitamin D in the human body. | Rickets is a disease caused by a vitamin D deficiency. Vitamin D can be obtained from ultra violet radiation and from various food sources. Cytochrome P450 enzymes are involved in the first step to regulate and process vitamin D in the human body. | ||
<scene name='48/483888/Human_p450/1'>Human P450</scene> | |||
==Overall Structure== | ==Overall Structure== | ||
Revision as of 20:07, 5 March 2016
| 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. |
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 <StructureSection load='3c6g' size='350' side='right' caption='caption for Molecular Playground (PDB entry 3c6g)' scene=>
Introduction
Rickets is a disease caused by a vitamin D deficiency. Vitamin D can be obtained from ultra violet radiation and from various food sources. Cytochrome P450 enzymes are involved in the first step to regulate and process vitamin D in the human body. Human P450
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
Secondary Structure -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 this orientation 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
