Rapamycin: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
(One intermediate revision by the same user not shown) | |||
Line 2: | Line 2: | ||
==Structure== | ==Structure== | ||
<StructureSection load=' | <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/ | 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] |
|
ReferencesReferences
- ↑ https://en.wikipedia.org/wiki/Sirolimus
- ↑ https://doi.org/10.3389/fphar.2016.00395
- ↑ 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