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Ligand Binding Sites

Ligand Binding Sites

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Updated: Jan 6, 2026

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

The APEXTAC System for Ligand-Guided Proximity Labeling.

Min Ma¹, YiYu Wang¹, Johannes E Koeckenberger¹

¹Department of Chemistry and Biochemistry, University of California San Diego, San Diego, CA, 92093, USA.

Chembiochem : a European Journal of Chemical Biology

|November 2, 2025

Summary

This summary is machine-generated.

The new APEXTAC system enables unbiased drug-target identification in live cells. It overcomes BioTAC limitations, offering faster labeling and improved accuracy for protein homeostasis research.

Keywords:

APEX2 TargetID proximity labeling

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Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

Published on: September 20, 2016

Area of Science:

Chemical Biology
Molecular Biology
Drug Discovery

Background:

Unbiased drug-target identification is crucial for understanding drug mechanisms and off-target effects.
Existing methods like BioTAC have limitations, including specific chemistry and labeling duration.
The need for improved proximity labeling tools in live-cell studies is evident.

Purpose of the Study:

To develop and validate the APEXTAC system, a novel small molecule-guided proximity labeling platform.
To compare APEXTAC head-to-head with the BioTAC system for drug-target identification.
To assess APEXTAC's utility in studying protein homeostasis and targeted protein degradation.

Main Methods:

Development of the APEXTAC system utilizing the APEX2 peroxidase enzyme.
Head-to-head comparison of APEXTAC and BioTAC using (+)-JQ1 for target identification.
Assessment of labeling efficiency and specificity in live cells.

Main Results:

APEXTAC successfully labeled E3-ligases via their ligands without proteasome inhibitors.
The APEXTAC system demonstrated faster and potentially more accurate target identification compared to BioTAC.
APEXTAC proved effective for live-cell target identification across various molecules, including protein homeostasis components.

Conclusions:

APEXTAC is a valuable complementary tool for unbiased live-cell drug-target identification.
The system overcomes key limitations of previous proximity labeling methods.
APEXTAC shows significant potential for applications in targeted protein degradation research.