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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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  1. Home
  3. Linker-driven Sampling Of Protac-induced Ternary Complexes.
  1. Home
  3. Linker-driven Sampling Of Protac-induced Ternary Complexes.

Related Experiment Video

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)
07:22

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)

Published on: January 12, 2024

Linker-Driven Sampling of PROTAC-Induced Ternary Complexes.

Hongtao Zhao1, Stefan Schiesser1, Christian Tyrchan1

  • 1Biopharma Chemistry, Discovery Sciences, BioPharmaceuticals R&D, AstraZeneca, Gothenburg 43183, Sweden.

Journal of Medicinal Chemistry
|June 3, 2026

View abstract on PubMed

Summary
This summary is machine-generated.

This study introduces TERNIFY, a computational method for modeling ternary complexes crucial for Proteolysis-Targeting Chimeras (PROTACs) drug design. The software efficiently predicts complex structures, aiding in the development of novel therapeutics.

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Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay
06:17

Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay

Published on: February 28, 2025

Related Experiment Videos

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)
07:22

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)

Published on: January 12, 2024

Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay
06:17

Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay

Published on: February 28, 2025

Area of Science:

  • Biochemistry
  • Computational Chemistry
  • Drug Discovery

Background:

  • Proteolysis-targeting chimeras (PROTACs) are heterobifunctional molecules inducing targeted protein degradation.
  • Formation of the ternary complex (PROTAC-E3 ligase-protein of interest) is critical for PROTAC efficacy.
  • Structural understanding of ternary complexes is vital for rational PROTAC design.

Purpose of the Study:

  • To develop and validate a computational approach for sampling PROTAC-induced ternary complexes.
  • To create an open-source software tool, TERNIFY, for streamlined ternary complex modeling.

Main Methods:

  • A computational method reducing search space to linker conformational degrees of freedom.
  • Validation using 40 cocrystal ternary complex structures.
  • Testing with unbound protein structures for WDR5-PROTAC-VHL complexes.

    • Main Results:

    • Achieved 97% and 50% retrospective success rates at Cα-RMSD thresholds of 10 and 4 Å, respectively.
    • Predicted ternary complexes were within 7 Å of experimental structures for WDR5-PROTAC-VHL complexes.
    • TERNIFY enables standalone ternary complex modeling without separate docking steps.

    Conclusions:

    • The computational approach effectively samples PROTAC-induced ternary complexes.
    • TERNIFY provides an efficient, integrated workflow for ternary complex modeling.
    • This tool facilitates rational PROTAC design and accelerates therapeutic development.