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/Protein_view_1/1'>PYCR1 is an enzyme found in humans. It is a potential cancer therapy target. In this variation of the protein, the analog THFA binds to the enzyme PYCR1 and works as a weak inhibitor. PYCR1 is the enzyme that reverses the intermediate Pyrroline 5-carboxylate (P5C) in Proline synthesis. </scene>
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<scene name='87/873229/Protein_view_1/1'>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>
== Biological relevance and broader implications ==
== Biological relevance and broader implications ==
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Because cancer cells increase proline numbers when THFA is present within PYCR1, it binds to areas that proline would normally bind because of its size, shape, and noncovalent bonds. When THFA binds to PYCR1, the enzyme is able to act as an inhibitor. This could be an important finding in breast cancer research.
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Because cancer cells increase proline numbers when THFA is present within PYCR1, it binds to areas that proline would normally bind because of THFA's similarity to proline in size, shape, and noncovalent bonds. When THFA binds to PYCR1, the ligand is able to act as an inhibitor. This could be an important finding in breast cancer research.
== Important amino acids==
== Important amino acids==
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<scene name='87/873229/Ligand_view/1'>Important amino acids in the ligand THFA are Ser233, Val231, Thr238, Ala237.</scene>
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<scene name='87/873229/Ligand_view/2'>THFA is a proline analog inhibitor that contains the amino acids Ser233, Val231, Thr238, and Ala237 within its structure.</scene> <scene name='87/873229/Ligand_water/1'>This image shows the Oxygen binding of THFA. </scene>
== Structural highlights ==
== Structural highlights ==
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<scene name='87/873229/Alpha_helix/1'>These are the alpha helix in PYCR1 highlighted in black.</scene>
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<scene name='87/873229/Beta_sheet/1'>These are the beta sheets in PYCR1 highlighted in red. </scene>
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<scene name='87/873229/Alpha_and_beta/1'>These are the alpha helix (black) and beta sheets (red) in PYCR1. </scene>
== Other important features ==
== Other important features ==

Revision as of 14:39, 16 April 2021

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.
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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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