User:Tori Templin/Sandbox 1
From Proteopedia
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ACAT is a dimer of dimers, which is also known as a [https://en.wikipedia.org/wiki/Tetramer tetramer]. | ACAT is a dimer of dimers, which is also known as a [https://en.wikipedia.org/wiki/Tetramer tetramer]. | ||
This | This | ||
| - | <scene name='87/877604/Tetramer/ | + | <scene name='87/877604/Tetramer/2'>tetramer</scene> |
is about 260 kDa and is composed completely of helices, with each monomer containing 9 transmembrane helices. | is about 260 kDa and is composed completely of helices, with each monomer containing 9 transmembrane helices. | ||
The | The | ||
Revision as of 20:10, 30 March 2021
Acyl-Coenzyme A Cholesterol Acyltransferase
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References
- ↑ Farese RV Jr. The nine lives of ACAT inhibitors. Arterioscler Thromb Vasc Biol. 2006 Aug;26(8):1684-6. doi:, 10.1161/01.ATV.0000227511.35456.90. PMID:16857957 doi:http://dx.doi.org/10.1161/01.ATV.0000227511.35456.90
- ↑ Guan C, Niu Y, Chen SC, Kang Y, Wu JX, Nishi K, Chang CCY, Chang TY, Luo T, Chen L. Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor. Nat Commun. 2020 May 18;11(1):2478. doi: 10.1038/s41467-020-16288-4. PMID:32424158 doi:http://dx.doi.org/10.1038/s41467-020-16288-4
- ↑ Qian H, Zhao X, Yan R, Yao X, Gao S, Sun X, Du X, Yang H, Wong CCL, Yan N. Structural basis for catalysis and substrate specificity of human ACAT1. Nature. 2020 May;581(7808):333-338. doi: 10.1038/s41586-020-2290-0. Epub 2020 May, 13. PMID:32433614 doi:http://dx.doi.org/10.1038/s41586-020-2290-0
Student Contributors
- Tori Templin
- Haylie Moehlenkamp
- Megan Fleshman
