User:Tori Templin/Sandbox 1

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Revision as of 20:04, 23 March 2021

Acyl-Coenzyme A Cholesterol Acyltransferase

spinqualitylabelsall models ACAT Tetramer Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image [1] Contents 1 Introduction 2 Function 3 Disease 4 Structural highlights 5 Relevance Introduction Acyl-Coenzyme A Cholesterol Acyltransferase (ACAT), or also known as Sterol O-Acyltransferase (SOAT), is an important enzyme in the body. Figure 1. ACAT as a Dimer of Dimers Function ACAT is an important enzyme that catalyzes the esterification of cholesterol to form cholesterol esters. SOAT article [2] ACAT article [3] Disease atherosclerosis, Alzheimer's Disease Structural highlights tetramer Relevance talk about inhibitor CI-976 Image:CI-976 Figure 2. CI-976 Inhibitor

References

1. ↑ 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
2. ↑ 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
3. ↑ 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