User:Sean Callahan/Sandbox 1
From Proteopedia
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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. | ||
| - | == | + | ==Introduction=== |
| - | + | Histones are positively charged proteins that help organize DNA into tightly packed chromosomes by acting as a spool for DNA to wrap around. Histones have the capability to loosen or tighten their interactions with DNA to either promote or inhibit transcription. There are a variety of mechanisms that histones achieve these interactions, some examples being the addition or removal of acetyl, methyl, or phosphate groups. These modifications can either increase or decrease the affinity the histone has for the DNA strand. Demethylase proteins are responsible for removing methyl groups from different histone residues. While this is typically associated with increasing histone-DNA interaction, and thus silencing transcription, demethylation has also been associated with the promotion of transcription depending on the residue that is being demethylated. | |
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| - | The | + | There are two main classes of demethylase proteins and they are categorized by their co-factors and co-substrates. One class of demethylases uses an FAD co-factor to catalyze the demethylation reaction. The other class of demethylases uses a FE+2 ion and a-ketoglutarate as a co-substrate to catalyze the reaction. Although the co-factors used are different, both classes operate by hydroxylating the target methyl group. Lysine Specific Demethylase 1 |
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| - | <scene name='81/811710/Oxidase/1'>Oxidase Domain</scene> | ||
| - | == Disease == | ||
| - | [https://www.cdc.gov/diseasesconditions/index.html Seans fav link] | ||
| - | == Relevance == | ||
| - | == Structural highlights == | ||
| - | 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> | ||
Revision as of 18:51, 5 April 2019
=Lysine Specific Demethylase 1 (Homo sapiens)=
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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
- ↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677
- ↑ Mineo R, Sharrock NE. Venous levels of lidocaine and bupivacaine after midtarsal ankle block. Reg Anesth. 1992 Jan-Feb;17(1):47-9. PMID:1599895
