Sandbox Reserved 1667
From Proteopedia
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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='6XOZ' size='340' side='right' caption='Caption for this structure' scene=''> | <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. | ||
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== Function of your protein == | == Function of your protein == | ||
| - | <scene name='87/873229/ | + | <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 == | ||
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== Important amino acids== | == 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/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> | ||
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== Structural highlights == | == Structural highlights == | ||
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== Other important features == | == Other important features == | ||
| - | <scene name= | + | <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> | ||
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
