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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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Structural basis for FGF receptor dimerization and activation.

A N Plotnikov1, J Schlessinger, S R Hubbard

  • 1Department of Pharmacology, New York University School of Medicine, New York 10016, USA.

Cell
|September 18, 1999
PubMed
Summary
This summary is machine-generated.

The crystal structure reveals how Fibroblast Growth Factor 2 (FGF2) binds Fibroblast Growth Factor Receptor 1 (FGFR1), forming a dimer. This structure explains FGF- and heparin-induced receptor dimerization.

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Area of Science:

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Fibroblast Growth Factor 2 (FGF2) is crucial for cell signaling.
  • Fibroblast Growth Factor Receptor 1 (FGFR1) mediates FGF2 signaling.
  • Understanding FGF2-FGFR1 interactions is key to deciphering cell growth and differentiation pathways.

Purpose of the Study:

  • To determine the crystal structure of FGF2 bound to immunoglobulin-like domains 2 and 3 (D2 and D3) of FGFR1.
  • To elucidate the molecular mechanisms underlying FGF2-FGFR1 complex formation and dimerization.
  • To provide a structural basis for FGF- and heparin-induced FGFR dimerization.

Main Methods:

  • X-ray crystallography at 2.8 A resolution.
  • Analysis of the FGF2:FGFR1 complex structure.
  • Identification of interaction interfaces and potential heparin-binding sites.

Main Results:

  • The crystal structure reveals a 2-fold symmetric dimer formed by two FGF2:FGFR1 complexes.
  • FGF2 interacts extensively with FGFR1 domains D2 and D3, and the inter-domain linker.
  • A positively charged canyon on FGFR1 is identified as a potential heparin-binding site.
  • Dimer stabilization involves interactions between FGF2, D2 domains, and inter-receptor D2-D2 contacts.

Conclusions:

  • The crystal structure provides a detailed molecular model of the FGF2-FGFR1 complex.
  • The findings offer insights into the mechanism of FGF- and heparin-mediated FGFR dimerization.
  • This structural understanding unifies existing biochemical data and supports a general model for receptor activation.