User:Andrew Hesterhagen/Sandbox 1

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LSD-1 can be regulated by outside factors. The tower domain and oxidase domain are connected by a <scene name='81/811710/Tower_domain/1'>tower oxidase domain</scene>. The oxidase domain is what harbors the catalytic chamber for LSD-1. Any change to the catalytic chamber could drastically reduce the ability for the methylated lysine of the substrate to fit in the binding site correctly. Because the tower domain is attached to the oxidase domain, the tower domain and the connector region may allosterically regulate demethylase activity. Any interaction with these two sites is hypothesized to change the enzyme activity. This has further pushed the assumption that the CoRest complex effects enzyme activity via interaction with the tower domain.<ref>PMID:16799558</ref>
LSD-1 can be regulated by outside factors. The tower domain and oxidase domain are connected by a <scene name='81/811710/Tower_domain/1'>tower oxidase domain</scene>. The oxidase domain is what harbors the catalytic chamber for LSD-1. Any change to the catalytic chamber could drastically reduce the ability for the methylated lysine of the substrate to fit in the binding site correctly. Because the tower domain is attached to the oxidase domain, the tower domain and the connector region may allosterically regulate demethylase activity. Any interaction with these two sites is hypothesized to change the enzyme activity. This has further pushed the assumption that the CoRest complex effects enzyme activity via interaction with the tower domain.<ref>PMID:16799558</ref>
===Androgen Receptor===
===Androgen Receptor===
-
LSD-1 will demethylate mono or di-methylated lysines. It will only demethylate lysine 4 of histone 3. This factor can be regulated by the androgen receptor which can change its specificity for a different target. The [http://proteopedia.org/wiki/index.php/Androgen_receptor#Function androgen receptor] is a steroid hormone receptor that can modulate transcription. When it interacts with LSD-1 it will no longer demethylate H3-K4, but will now demethylate H3-K9. This attribute allows LSD-1 to work on a wider range of residues.<ref>PMID:16799558</ref>
+
LSD-1 will demethylate mono or di-methylated lysines. It will only demethylate lysine 4 of histone 3. This factor can be regulated by the androgen receptor which can change its specificity for a different target.<ref>PMID:16799558</ref> The [http://proteopedia.org/wiki/index.php/Androgen_receptor#Function androgen receptor] is a steroid hormone receptor that can modulate transcription. When it interacts with LSD-1 it will no longer demethylate H3-K4, but will now demethylate H3-K9. This attribute allows LSD-1 to work on a wider range of residues.<ref>PMID:16799558</ref>
== Relevance ==
== Relevance ==
<scene name='81/811710/Fad_n5/3'>No merc</scene>
<scene name='81/811710/Fad_n5/3'>No merc</scene>

Revision as of 17:58, 19 April 2019

=Lysine Specific Demethylase (Homo Sapiens)=

Your Heading Here (maybe something like 'Structure')

Lysine Demthylase (PDB entry 2h94)

Drag the structure with the mouse to rotate

References

[6] [7] [8]

  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
  3. ↑ Stavropoulos P, Blobel G, Hoelz A. Crystal structure and mechanism of human lysine-specific demethylase-1. Nat Struct Mol Biol. 2006 Jul;13(7):626-32. Epub 2006 Jun 25. PMID:16799558 doi:10.1038/nsmb1113
  4. ↑ Stavropoulos P, Blobel G, Hoelz A. Crystal structure and mechanism of human lysine-specific demethylase-1. Nat Struct Mol Biol. 2006 Jul;13(7):626-32. Epub 2006 Jun 25. PMID:16799558 doi:10.1038/nsmb1113
  5. ↑ Stavropoulos P, Blobel G, Hoelz A. Crystal structure and mechanism of human lysine-specific demethylase-1. Nat Struct Mol Biol. 2006 Jul;13(7):626-32. Epub 2006 Jun 25. PMID:16799558 doi:10.1038/nsmb1113
  6. ↑ 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
  7. ↑ 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
  8. ↑ Stavropoulos P, Blobel G, Hoelz A. Crystal structure and mechanism of human lysine-specific demethylase-1. Nat Struct Mol Biol. 2006 Jul;13(7):626-32. Epub 2006 Jun 25. PMID:16799558 doi:10.1038/nsmb1113

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Andrew Hesterhagen

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