Rapamycin: Difference between revisions

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==Structure==
==Structure==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='' size='340' side='right' caption='' scene='82/821566/Rapamycin/3'>
[[Image:Rapamycin.png]]
[[Image:Rapamycin.png]]


Rapamycin, a macrolide, has a <scene name='82/821566/Rapamycin/1'>cyclic structure</scene>. It <scene name='82/821566/Rapamycin/2'>binds to the regulator protein mTORC1</scene> with the help of another protein called FKBP52<ref>PMID: 23358420</ref>
Rapamycin, a macrolide, has a <scene name='82/821566/Rapamycin/3'>cyclic structure</scene>. It <scene name='82/821566/Rapamycin/2'>binds to the regulator protein mTORC1</scene> with the help of another protein called FKBP52<ref>PMID: 23358420</ref>
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 17:27, 17 July 2019

Rapamycin, isolated from the bacterium Streptomyces hygroscopicus, is an immuno-suppressant and anticancer drug[1]. It acts by binding the the mTORC1 protein complex, a kinase that regulates cell growth and metabolism. In the future, it might also be used in treatment of type 2 diabetes[2].

StructureStructure

Rapamycin, a macrolide, has a . It with the help of another protein called FKBP52[3]

Drag the structure with the mouse to rotate

ReferencesReferences

  1. https://en.wikipedia.org/wiki/Sirolimus
  2. https://doi.org/10.3389/fphar.2016.00395
  3. Marz AM, Fabian AK, Kozany C, Bracher A, Hausch F. Large FK506-binding Proteins Shape the Pharmacology of Rapamycin. Mol Cell Biol. 2013 Jan 28. PMID:23358420 doi:http://dx.doi.org/10.1128/MCB.00678-12

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Karsten Theis