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Updated: Jul 2, 2026
11:54
Real-Time Proxy-Control of Re-Parameterized Peripheral Signals using a Close-Loop Interface
Published on: May 8, 2021
Built-in loops allow versatility in domain-domain interactions: lessons from self-interacting domains
Eyal Akiva1, Zohar Itzhaki, Hanah Margalit
1Department of Molecular Genetics and Biotechnology, Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem 91120, Israel.
Summary
Researchers identified specific surface loops that control whether protein domains interact or remain separate. These enabling and disabling loops are evolutionarily conserved, impacting protein-protein interaction prediction.
Area of Science:
- Protein structure and function
- Molecular biology
- Evolutionary biology
Background:
- Protein-protein interactions are crucial for cellular processes.
- Domain-domain interactions mediate many protein interactions, but not all potential interactions occur.
- Sub-domain features may regulate these interactions.
Purpose of the Study:
- To identify structural and sequence features below the domain level that determine protein-protein interaction potential.
- To investigate the role of surface loops in mediating or preventing domain-mediated homodimerization.
Main Methods:
- Comparative analysis of protein domains involved in homodimerization versus those found in monomers.
- Identification and characterization of surface loops within these domains.
- Analysis of evolutionary conservation of identified loops.
Main Results:
- Discovery of 'enabling loops' that mediate domain interactions.
- Discovery of 'disabling loops' that prevent domain interactions.
- High evolutionary conservation of these enabling and disabling loops was observed.
Conclusions:
- Surface loops act as key determinants for protein-domain interaction specificity.
- Evolution preserves both interaction-promoting and interaction-inhibiting elements.
- These findings enhance the prediction of protein-protein interactions by highlighting critical regulatory regions.
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