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The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

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ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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Structure of Carboxylic Acid Derivatives
Carboxylic acid derivatives contain an acyl group attached to a heteroatom such as chlorine, oxygen, or nitrogen. The carbonyl carbon and oxygen are both sp2-hybridized with an unhybridized p orbital.
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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
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Related Experiment Video

Updated: Dec 21, 2025

Author Spotlight: Exploring Cellular Processes by Modeling Ligands in Cryo-EM Maps
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Structure of nevanimibe-bound tetrameric human ACAT1.

Tao Long1, Yingyuan Sun1, Abdirahman Hassan1

  • 1Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX, USA.

Nature
|May 21, 2020
PubMed
Summary

The structure of human ACAT1, an enzyme crucial for cholesterol homeostasis, was determined using cryo-electron microscopy. This reveals how ACAT1 interacts with inhibitors like nevanimibe, aiding in disease treatment development.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • Cholesterol is vital for cell membranes but tightly regulated in the endoplasmic reticulum (ER).
  • The ER enzyme sterol O-acyltransferase 1 (ACAT1) manages cholesterol levels by forming cholesteryl esters.
  • ACAT1 dysregulation is linked to Alzheimer's, atherosclerosis, and cancers.

Purpose of the Study:

  • To elucidate the structural basis of ACAT1 function and inhibition.
  • To understand the interaction between ACAT1 and its inhibitor, nevanimibe.
  • To provide insights for developing novel ACAT1-targeting therapeutics.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structure of human ACAT1.
  • Biochemical analyses were performed to study enzyme activity and inhibitor binding.
  • Structural data was integrated with existing knowledge of ACAT1 catalytic mechanisms.

Main Results:

  • The cryo-EM structure reveals ACAT1 as a tetramer comprising two homodimers.
  • A central cavity within the ACAT1 monomer accommodates the inhibitor nevanimibe and acyl-coenzyme A.
  • Key interactions between ACAT1, nevanimibe, and the catalytic histidine residue were identified.

Conclusions:

  • The study provides a detailed structural model for cholesterol esterification by ACAT1.
  • The findings illuminate the molecular interactions underlying ACAT1 inhibition by nevanimibe.
  • This structural understanding can accelerate the development of ACAT1 inhibitors for various diseases.