User:Tori Templin/Sandbox 1: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 19: Line 19:
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].  
The  
The  
<scene name='87/877604/Colored_dimer/2'>Dimer of ACAT</scene>
<scene name='87/877604/Colored_dimer/2'>dimer of ACAT</scene>
was found to be the active arrangement.
was found to be the active arrangement.
<scene name='87/877604/Practice2/1'>protein orientation</scene>
<scene name='87/877604/Practice2/1'>protein orientation</scene>
The  
The  
<scene name='87/877604/Dimer_interface/1'>Dimer-Dimer Interface</scene>
<scene name='87/877604/Dimer_interface/1'>dimer-dimer interface</scene>
is mobile and mostly hydrophobic.
is mobile and mostly hydrophobic.


Revision as of 22:29, 30 March 2021

Acyl-Coenzyme A Cholesterol AcyltransferaseAcyl-Coenzyme A Cholesterol Acyltransferase

Introduction

Acyl-Coenzyme A Cholesterol Acyltransferase (ACAT), or also known as Sterol O-Acyltransferase (SOAT), is an important enzyme in the body.

Cholesterol esters were discovered in arterial lesions in 1910. Between 1980-1995, the interest in ACAT inhibitors grew, but some of the compounds looked at exhibited toxicity. In 1993, an ACAT gene was successfully cloned. This discovery led to more studies with ACAT and atherosclerosis. [1] add more history

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

ACAT is a dimer of dimers, which is also known as a tetramer.

The was found to be the active arrangement. The is mobile and mostly hydrophobic.

Relevance

talk about inhibitor CI-976

Figure 2. CI-976 Inhibitor

ACAT Tetramer

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ 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
  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 ContributorsStudent Contributors

  • Tori Templin
  • Haylie Moehlenkamp
  • Megan Fleshman
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=User:Tori_Templin/Sandbox_1&oldid=3374772"