Sandbox Reserved 1667
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{{Sandbox_Reserved_BHall_Sp21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_BHall_Sp21}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | == | + | ==Structure of Human PYCR1 with THFA Complex== |
| - | <StructureSection load=' | + | <StructureSection load='6XOZ' size='340' side='right' caption='Caption for this structure' scene=''> |
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| - | == Function == | + | == Function of your protein == |
| + | <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 == |
| + | 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== | ||
| + | <scene name='87/873229/All_ligands/1'>This shows all 5 THFA ligands.</scene> <scene name='87/873229/Ligand_view/2'>THFA is a proline analog inhibitor that interacts with the amino acids Ser233, Val231, Thr238, and Ala237 within the PYCR1 structure.</scene> <scene name='87/873229/Ligand_water/1'>This image shows the Oxygen binding of THFA.</scene> | ||
| + | <scene name='87/873229/Important_amino_acids/1'>Ser233, Val231, Thr238, and Ala237 within the PYCR1 structure.</scene> | ||
| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
| + | <scene name='87/873229/Alpha_helix/2'>These are the alpha helix in PYCR1 highlighted in dark blue. </scene> | ||
| + | <scene name='87/873229/Beta_sheet/2'>These are the beta sheets in PYCR1 highlighted in red. </scene> | ||
| + | <scene name='87/873229/Alpha_beta/1'>These are the alpha helix and beta sheets in PYCR1 highlighted in light blue with the other structures and ligands highlighted in maroon.</scene> | ||
| + | <scene name='87/873229/Tertiary_structures/1'>Chain E tertiary structure.</scene> | ||
| + | <scene name='87/873229/Quaternary_structure/1'>Protein quarternary structure.</scene> | ||
| + | |||
| - | + | == Other important features == | |
| + | <scene name='87/873229/Hydrophobic_polar/1'>Hydrophobic areas in grey. Polar areas in purple. Proline is hydrophobic so would need to bind in hydrophobic areas. </scene> | ||
| + | <scene name='87/873229/Proline/1'>Prolines highlighted in black.</scene> | ||
| + | <scene name='87/873229/Proline_and_hydrophobic/1'>Proline against hydrophobic areas.</scene> | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| + | <ref>33109600</ref> | ||
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. |
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Structure of Human PYCR1 with THFA Complex
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References
- ↑ 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
- ↑ 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
