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Modularity in the TNF-receptor family

J H Naismith1, S R Sprang

  • 1Centre for Biomolecular Sciences, University, St Andrews, Scotland, UK. naismith@st-andrews.ac.uk

Trends in Biochemical Sciences
|April 16, 1998
PubMed
Summary

Tumour necrosis factor (TNF) receptor family proteins regulate cell death and proliferation. Their extracellular domains are built from two distinct polypeptide modules, influencing receptor structure and function.

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Area of Science:

  • Structural biology
  • Molecular and cell biology

Background:

  • Tumour necrosis factor (TNF) receptor family members are crucial regulators of cellular processes, including proliferation and programmed cell death.
  • The extracellular domains of these receptors contain small, cysteine-rich subdomains, initially characterized in type I TNF receptor structures.

Purpose of the Study:

  • To analyze the structural organization of the extracellular domains of TNF receptor family members.
  • To identify conserved structural modules within these domains and their potential roles.

Main Methods:

  • Structure-based sequence alignment of TNF receptor family members.
  • Analysis of three-dimensional structures of TNF receptors.

Main Results:

  • The extracellular domains of TNF receptor family members are primarily composed of two small polypeptide modules.
  • These modules have distinct structural functions within the domain architecture.
  • Similar modules are found in other receptor and extracellular protein domains.

Conclusions:

  • The identified polypeptide modules provide a fundamental framework for TNF receptor extracellular domain structure.
  • Variations in module sequence and assembly explain differences in receptor shape, flexibility, and ligand specificity.
  • This modular organization is conserved across various receptor types.

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