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This research aims to understand how mutations affect binding energy and stability in homologous proteins, specifically in PDZ domains.

April 23, 2026Nature Communications2 citationsOpen Access

Comparative Maps of Allosteric Mutations in PDZ Domain Proteins

Seven complete comparative maps of allosteric mutations in a protein family

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Comprehensive maps reveal binding energy changes in PDZ domains, suggesting unique allosteric drug targets.

This research aims to understand how mutations affect binding energy and stability in homologous proteins, specifically in PDZ domains.
Constructed seven maps of mutations affecting binding and stability in five human PDZ domains.
Quantified 21,802 free energy changes, including binding energy and fold stability alterations.
Identified allosteric mutations and their impact on energy communication within the protein family.
Mapped 21,802 free energy changes, detailing 9064 in fold stability and 12,738 in binding energy.
Found a conserved decay in energetic effects of mutations away from binding interfaces across proteins.
Identified protein-specific allosteric mutations that suggest distinct targets for drug development.

Martí-Aranda et al. (2026) studied this question.

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April 23, 2026Nature Communications2 citationsOpen Access

Seven complete comparative maps of allosteric mutations in a protein family

View Full Paper

Ask AI

Bookmark

Authors

Comprehensive maps reveal binding energy changes in PDZ domains, suggesting unique allosteric drug targets.

This research aims to understand how mutations affect binding energy and stability in homologous proteins, specifically in PDZ domains.
Constructed seven maps of mutations affecting binding and stability in five human PDZ domains.
Quantified 21,802 free energy changes, including binding energy and fold stability alterations.
Identified allosteric mutations and their impact on energy communication within the protein family.
Mapped 21,802 free energy changes, detailing 9064 in fold stability and 12,738 in binding energy.
Found a conserved decay in energetic effects of mutations away from binding interfaces across proteins.
Identified protein-specific allosteric mutations that suggest distinct targets for drug development.

Martí-Aranda et al. (2026) studied this question.

View Full Paper

Ask AI

Bookmark