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Assembly of Signaling Complexes01:30

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Updated: Jun 22, 2026

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
10:05

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

A sequential binding mechanism in a PDZ domain.

Celestine N Chi1, Anders Bach, Ake Engström

  • 1Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, SE-75123 Uppsala, Sweden.

Biochemistry
|June 6, 2009
PubMed
Summary
This summary is machine-generated.

The PDZ2 domain of SAP97 protein binds ligands through an induced fit mechanism, not conformational selection. This involves a two-step process with a precomplex intermediate, confirmed by kinetic binding experiments.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Allosteric protein-ligand interactions are crucial in biological systems.
  • Conformational selection and induced fit are established interaction mechanisms.
  • Single-domain proteins like ubiquitin may utilize conformational selection.

Purpose of the Study:

  • To investigate the binding mechanism of the SAP97 PDZ2 domain with peptide ligands.
  • To determine if PDZ2 utilizes conformational selection or induced fit for ligand binding.

Main Methods:

  • Performed binding experiments using SAP97 PDZ2 and peptide ligands.
  • Utilized stopped-flow technique to observe kinetics.
  • Employed an ultrarapid continuous-flow mixer to analyze binding rates.

Main Results:

  • Observed biphasic kinetics, indicating a multi-step binding process.
  • Detected hyperbolic dependence of rate constants on peptide concentration, supporting a two-step mechanism.
  • Demonstrated that PDZ2-peptide interaction involves a precomplex followed by conformational change.

Conclusions:

  • The PDZ2 domain of SAP97 binds ligands via a sequential induced fit mechanism.
  • This finding contrasts with the proposed general applicability of conformational selection for single-domain proteins.
  • The interaction proceeds through a precomplex intermediate that undergoes conformational adaptation.