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Sandbox GGC3
From Proteopedia
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| - | + | ==Your Heading Here (maybe something like 'Structure')== | |
| - | <StructureSection load='4ZRA' size='340' side='right' caption='Caption for this structure' scene=' | + | <StructureSection load='4ZRA' size='340' side='right' caption='Caption for this structure' scene=''> |
| - | + | This is a default text for your page '''Sandbox GGC3'''. 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. | |
== Function == | == Function == | ||
| - | Macromolecule LprG biochemical function is binding and transportation. For binding it interacts selectively and noncovalently with glycerophospholipids and phosphorylated derivatives. As for transportation LprG binds triacylglyceride (TAG) in a large hydrophobic cleft and transfers TAG from donor to acceptor membranes. <ref name="rasmol">PMID: 26751071</ref> | ||
== Disease == | == Disease == | ||
| - | Tuberculosis is an infectious disease that is the second leading cause of death worldwide. Mycobacterium tuberculosis is an intracellular bacterial pathogen in infected macrophages. It contributes to antibiotic resistance and plays a critical role in regulating host response and aid survival of pathogen. LprG determines the components of mycobacterium tuberculosis cell envelope. <ref name="rasmol" /> | ||
| + | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
| - | LprG (4ZRA) consists of two chains A and C containing alpha-beta folds. <scene name='75/752266/Sheets_and_helices/1'>Chain A </scene> contains 10 anti-parallel ß-sheets with 6 α-helices which defines the central cavity entrance. The <scene name='75/752266/Sheets_and_helices/2'>glyceryl group</scene> is located at the entrance. At the cavity entrance the hydrophilic glyceryl interacts with <scene name='75/752266/Sn3-chain/3'> Ser72 </scene>. There are three acyl chains on the ligand bound within the cavity sn1, sn2, and <scene name='75/752266/Ligand_strutuce_alone/2'>sn3</scene> they form interactions with hydrophobic residue side chains within the cavity. The <scene name='75/752266/Surface/1'>third acyl</scene> chain is exposed to the solvent and the other two (sn1 and sn2) buried inside the LprG. The sn3 chain is near two <scene name='75/752266/Phe_leu_ile/3'>hydrophobic</scene> grooves that contain Ile, Leu, Val, and Phe. These grooves could facilitate the binding of TAG with other longer acyl chains.<ref name="rasmol" /> | ||
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| + | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
| - | |||
<references/> | <references/> | ||
Revision as of 18:55, 23 February 2018
Your Heading Here (maybe something like 'Structure')
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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
