What question did this study set out to answer?

To determine whether electrostatic interactions with the peptide terminus govern ligand recognition energetics and specificity in the mouse alpha1-syntrophin PDZ domain.

February 22, 2003Biochemistry

Role of Electrostatic Interactions in PDZ Domain Ligand Recognition

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Authors

BHBaruch Z. HarrisUniversity of California, San Francisco FLFrancis W. LauBoston University NFNaoaki FujiiPurdue University West Lafayette

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Implication

Biochemical analysis reveals minimal electrostatic contribution to ligand binding in mouse alpha1-syntrophin, indicating steric and hydrogen bonding determine specificity.

Key Points

To determine whether electrostatic interactions with the peptide terminus govern ligand recognition energetics and specificity in the mouse alpha1-syntrophin PDZ domain.
Assessed salt-dependent binding kinetics of the mouse alpha1-syntrophin PDZ domain against both terminal and internal peptide ligands.
Mutated a conserved basic residue implicated in electrostatic binding and performed chemical modification assays on ligand termini.
Direct electrostatic interactions involving the ligand carboxy terminus do not contribute significantly to the energetic drive of PDZ domain binding.
Ligand recognition specificity is primarily mediated by steric complementarity and hydrogen bonding networks, which both C-terminal and appropriately folded internal motifs can satisfy.

Cite This Study

Harris et al. (2003) studied this question.

synapsesocial.com/papers/6a717f29febe604dd70a2338 https://doi.org/10.1021/bi027061p

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Implication

Biochemical analysis reveals minimal electrostatic contribution to ligand binding in mouse alpha1-syntrophin, indicating steric and hydrogen bonding determine specificity.

Role of Electrostatic Interactions in PDZ Domain Ligand Recognition

Discussion

Member takes

Implication

Key Points

Cite This Study

Role of Electrostatic Interactions in PDZ Domain Ligand Recognition

Discussion

Member takes

Implication

Key Points

Cite This Study

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