Sandbox GGC1

From Proteopedia

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==Crystal structure of the tandem SAM domains from human SARM1==
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==Chymotrypsin==
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<StructureSection load='6O0S' size='340' side='right' caption='RNAse P Protein=''>
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox GGC1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
This is a default text for your page '''Sandbox GGC1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; 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 ==
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SARM1 is a protein that contains SAM and TIR domains. SARM1 is involved in the cleavage of NAD+. The SAM domains form an octamer and play a part in axon degeneration by contributing to the enzymatic activity of TIR, which will cleave NAD+.
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== Disease ==
== Disease ==
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The SAM domains are involved in Wallerian degeneration. In Wallerian degeneration, axons are degenerated following damage. This nerve damage can lead to neuropathic diseases. SARM1 also causes cell death in plants by cleaving NAD+.
 
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== Structural highlights ==
 
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The SAM domains need to form an octamer for SARM1 to be able to cleave NAD+. Five <scene name='75/752263/Important_hydrophobic_residues/2'>Amino Acids</scene> were found to be important for this to occur: Leu 442, Ile 461, Leu 514, Leu 531, and Val 533. These amino acids are found in <scene name='75/752263/Area_of_interest/1'>each of the eight domains</scene> that make up the octamer. <scene name='75/752263/Close_up_hydrophobic_residues/2'>If these amino acids</scene> were changed to arginine or aspartate, then NAD+ would no longer be able to be cleaved.
 
== Relevance ==
== Relevance ==
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If the five amino acids in the SAM domains that help form the octamer are changed to arginine or asparagine, then it may be possible to inhibit the function of SARM1 and thus stop or slow down neuropathies.
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== Structural highlights ==
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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 ==
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1. Horsefield, S., Burdett, H., Zhang, X., Manik, M. K., Shi, Y., Chen, J., … Kobe, B. (2019). NAD cleavage activity by animal and plant TIR domains in cell death pathways. Science, 365(6455), 793–799. doi: 10.1126/science.aax1911
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<references/>

Revision as of 09:46, 14 September 2020

Chymotrypsin

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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