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Interdomain interface-mediated target recognition by the Scribble PDZ34 supramodule.

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The PDZ34 tandem of Scribble forms a compact supramodule with an expanded binding groove. This interdomain interface is crucial for Scribble

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Tandem PDZ domains form supramodules with unique target-binding properties.
  • Scribble is a key regulator of cell polarity.
  • PDZ domains are crucial protein interaction modules.

Purpose of the Study:

  • To investigate the structural and functional properties of the PDZ34 tandem in Scribble.
  • To elucidate the target-binding mechanism of the Scribble PDZ34 supramodule.
  • To identify novel binding partners of Scribble.

Main Methods:

  • X-ray crystallography of the PDZ34-peptide complex.
  • Site-directed mutagenesis to probe the interdomain interface.
  • Analysis of target-binding capacity.

Main Results:

  • The PDZ34 tandem forms a compact supramodule via front-to-back packing.
  • An interdomain pocket is formed between PDZ3 and PDZ4, expanding the binding groove.
  • Peptide binding involves the interdomain pocket and PDZ3's canonical pocket.
  • Disruption of the interdomain interface abolishes target-binding capacity.

Conclusions:

  • The PDZ34 supramodule's interdomain interface is essential for target recognition and specificity.
  • This represents a novel mode of target recognition for PDZ supramodules.
  • Understanding this interaction can help identify Scribble's binding partners and polarity complex assembly.