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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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Related Experiment Video

Updated: Mar 17, 2026

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Published on: November 29, 2014

Mapping Lysine Acetyltransferase-Ligand Interactions by Activity-Based Capture.

D C Montgomery¹, J L Meier¹

¹Chemical Biology Laboratory, National Cancer Institute, Frederick, MD, United States.

Methods in Enzymology

|July 18, 2016

Summary

This summary is machine-generated.

Researchers developed new activity-based probes to profile lysine acetyltransferases (KATs). This method enables studying KAT interactions with ligands and offers insights into cellular KAT regulation.

Keywords:

Acetylation Activity-based probe Chemoproteomics Lysine acetyltransferase Metabolic regulation of epigenetics Profiling

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Last Updated: Mar 17, 2026

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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Reversible protein acetylation is crucial for genomic regulation and enzyme function.
Lysine acetyltransferases (KATs) catalyze this modification but are challenging to study due to complex structures.
Existing methods for KAT characterization are limited.

Purpose of the Study:

To develop novel methods for profiling endogenous KAT activities.
To enable the analysis of KAT interactions with various ligands, including acyl-CoA metabolites.
To assess ligand selectivity for different KAT families in complex biological systems.

Main Methods:

Development and application of activity-based probes (ABPs) for KAT profiling.
Utilizing a competitive activity-based capture approach.
Analysis of KAT-ligand interactions in proteomic settings.

Main Results:

Successfully profiled endogenous KAT activities using ABPs.
Demonstrated the ability to analyze interactions between KATs and diverse ligands.
Established a method to assess ligand selectivity across different KAT families.

Conclusions:

The developed ABP method facilitates targeted analysis of cellular KATs.
This approach provides substantial insights into the regulation of cellular KAT function.
Offers a powerful tool for drug discovery targeting KATs.