Order/Disorder Transitions Upon Protein Binding: A Unifying Perspective.

Area of Science:

• Biochemistry
• Structural Biology
• Bioinformatics

Background:

• Protein-protein interactions are fundamental to cellular processes.
• Binding events often induce significant conformational changes in protein structures.
• These structural changes can range from disorder to order or vice versa.

Purpose of the Study:

• To categorize the distinct possibilities of order/disorder transitions during protein binding.
• To identify experimentally observed and unobserved transition scenarios.
• To explore potential new examples of mutual synergistic folding using bioinformatics.

Main Methods:

• Analysis of the Protein Data Bank (PDB) for protein structural data.
• Bioinformatic approaches to identify specific binding-related order/disorder transitions.
• Classification of observed and unobserved transition types.

Main Results:

• Ten distinct types of binding-related order/disorder transitions were identified.
• Seven of these transition types have been previously reported or experimentally observed.
• Three transition types remain unobserved, with potential new examples of mutual synergistic folding identified.

Conclusions:

• Protein binding encompasses a diverse range of structural rearrangements.
• Mutual synergistic folding represents a notable mechanism where intrinsically disordered proteins gain structure upon complex formation.
• Bioinformatic analysis provides a powerful tool for discovering novel protein interaction mechanisms.