Sandbox Reserved 431
From Proteopedia
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- | ==''' | + | =='''Vitamin D activation by cytochrome P450, rickets (3c6g)<ref>PMID: 18511070 </ref>'''== |
by Isabel Hand, Elizabeth Humble, Kati Johnson, Samantha Kriksceonaitis, and Matthew Tiller | by Isabel Hand, Elizabeth Humble, Kati Johnson, Samantha Kriksceonaitis, and Matthew Tiller | ||
Revision as of 16:05, 25 February 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. |
Contents |
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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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
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from can you identify the green, red, and blue parts of the molecule?
See Also
Credits
Introduction - name of team member
Overall Structure - Kati Johnson
Drug Binding Site - name of team member
Additional Features - name of team member
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