Sandbox GGC9

From Proteopedia

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==Androgen receptor==
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==Your Heading Here (maybe something like 'Structure')==
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<StructureSection load='2Q7I' size='340' side='right' caption='androgen receptor' scene=''>
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<StructureSection load='3VEV' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox GGC9'''. 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 GGC9'''. 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.
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== Background ==
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== Function ==
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The androgen receptor (AR) is a member of the nuclear receptor superfamily of ligand-activated transcription factors. Androgen activation of AR regulates prostate growth, bone, muscle mass, and spermatogenesis. A ligand, usually testosterone, binds to the receptor and causes a conformational change to cause down stream effects.
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== ligands ==
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== Disease ==
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The ligands that have a high affinity to the AR are Testosterone (T) and Dihydrotestosterone (DHT). Testosterone is a cholesterol derivative, this hormone helps facilitate male maturation and development. Dihydrotestosterone is a tissue metabolite of testosterone and is significantly more potent then testosterone. <scene name='75/752271/1_ligand/1'>Testosterone Ball and stick</scene>
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==binding pocket==
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The way AR binds the dozens of coregulator proteins reported to associate with different regions of AR are poorly understood. Nuclear receptors activate transcription by binding short sequences such as LxxLL or FXXLF (where “x” is any amino acid). these residues bid to the OH group on the testosterone and allow for pocket stabilization.<scene name='75/752271/1_ar_b_pocket_alpha_c_labeled/3'>Androgen receptor binding pocket W/O ligand</scene>
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== Relevance ==
== Relevance ==
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the AR binds to testosterone to induce masculinization of males during the age of puberty. this allows for the development of male characteristics such as facial hair, deepening of the voice, sperm production and overall build. depending on the residue in the LXXLL motifs, the ligand binding may change. A FXXLF sequence mutation and a second N-terminal WXXLF sequence interact with different regions of the ligand binding site to stabilize the AR complex and may compete with AF2 recruitment of LXXLL motif-containing coactivators. The results suggest a unique mechanism for AR-mediated transcriptional activation.
 
== Structural highlights ==
== Structural highlights ==
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<scene name='75/752271/1_ar_b_pocket_alpha_c_labeled/2'>androgen recepto With ligand</scene>
 
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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.
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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.
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</StructureSection>
</StructureSection>
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== References ==
== References ==
<references/>
<references/>
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1. Askew EB, Gampe RT Jr, Stanley TB, Faggart JL, Wilson EM. Modulation of androgen receptor activation function 2 by testosterone and dihydrotestosterone. J Biol Chem. 2007;282(35):25801–25816. doi:10.1074/jbc.M703268200
 
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2. Hur E, Pfaff SJ, Payne ES, Grøn H, Buehrer BM, Fletterick RJ. Recognition and accommodation at the androgen receptor coactivator binding interface. PLoS Biol. 2004;2(9):E274. doi:10.1371/journal.pbio.0020274
 
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3.Davey, R. A., & Grossmann, M. (2016). Androgen Receptor Structure, Function and Biology: From Bench to Bedside. The Clinical biochemist. Reviews, 37(1), 3–15.
 

Revision as of 10:07, 14 September 2020

Your Heading Here (maybe something like 'Structure')

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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