Sandbox Reserved 1667

From Proteopedia

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== Function of your protein ==
== Function of your protein ==
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<scene name='87/873229/6xoz/10'>PYCR1 is a macromolecule found in humans. It is a potential cancer therapy target. In this variation of the protein, the enzyme THFA binds to the substrate PYCR1 and works as a weak inhibitor as THFA blocks the ability of proline to bind to the active site. PYCR1 reverses the intermediate Pyrroline 5-carboxylate (P5C) in Proline synthesis.</scene>
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<scene name='87/873229/6xoz/10'>PYCR1 is a macromolecule found in humans. It is a potential cancer therapy target. In this variation of the protein, the ligand THFA binds to PYCR1 and works as a weak inhibitor as THFA blocks the ability of proline to bind. PYCR1 reverses the intermediate Pyrroline 5-carboxylate (P5C) in Proline synthesis.</scene>
== Biological relevance and broader implications ==
== Biological relevance and broader implications ==

Current revision

This Sandbox is Reserved from 01/25/2021 through 04/30/2021 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1665 through Sandbox Reserved 1682.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Structure of Human PYCR1 with THFA Complex

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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