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Updated: Jul 17, 2026
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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
Published on: January 26, 2024
Continuous molecular evolution of protein-domain structures by single amino acid changes
Sebastian Meier1, Pernille R Jensen, Charles N David
1Department of Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. smeier@aki.ku.dk
Current Biology : CB
|January 24, 2007
Summary
Protein evolution may involve structural switches in cysteine-rich domains (CRDs). Single amino acid changes can alter CRD structures, potentially creating new protein folds and functions.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Protein structures are limited despite vast genetic information, leading to multifunctionality.
- The evolution of new protein structures and functions under these constraints is not well understood.
- Biomacromolecules may evolve by adopting multiple conformations, bridging different protein folds.
Purpose of the Study:
- To investigate how new protein structures and functions evolve.
- To explore the role of structural plasticity in molecular evolution.
- To demonstrate that single amino acid changes can induce global structural switches in protein domains.
Main Methods:
- Structure-based mutagenesis approach.
- Analysis of cysteine-rich domains (CRDs) in cnidarian nematocyst proteins.
- Investigating the ability of CRDs to form distinct structures with varying disulfide patterns.
Main Results:
- A global structural switch was observed in CRDs of cnidarian nematocyst proteins due to single amino acid changes.
- CRDs can interconvert between two native structures through a bridge state.
- Mutations stabilizing specific structures mimic the evolutionary emergence of new protein folds.
Conclusions:
- Single amino acid mutations can drive significant protein structural changes.
- This structural plasticity in CRDs provides a mechanism for evolving new protein folds and functions.
- The findings offer insights into the evolutionary pathways of protein diversity.
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A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
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Overview