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Related Experiment Video

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Exploring Adipose Tissue Structure by Methylsalicylate Clearing and 3D Imaging
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Structural polymorphism of oligomeric adiponectin visualized by electron microscopy.

Mazdak Radjainia1, Yu Wang, Alok K Mitra

  • 1School of Biological Sciences, University of Auckland, Postal Bag 92019, Auckland, New Zealand.

Journal of Molecular Biology
|July 11, 2008
PubMed
Summary

Adiponectin

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Medicine

Background:

  • Adiponectin exhibits diverse biological functions, including anti-diabetic, anti-atherosclerotic, anti-inflammatory, and anti-tumor activities.
  • These functions are linked to high molecular weight (HMW) oligomeric structures formed by adiponectin trimers.

Purpose of the Study:

  • To determine the 3-D structure of adiponectin trimers and hexamers.
  • To elucidate the structural basis for the formation and function of HMW adiponectin.

Main Methods:

  • Single-particle analysis of electron micrographs.
  • 3-D reconstruction of isolated recombinant murine C39A adiponectin trimer and wild-type hexamer.

Main Results:

  • Reconstructed two major classes of HMW adiponectin structures: fan-shaped (class I) and bouquet-shaped (class II).

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  • Identified a compact N-terminal volume crucial for HMW formation and dynamic C-terminal globular domains enabling ligand clustering.

    • Conclusions:

    • The N-terminal domain is essential for forming functionally active HMW adiponectin.
    • C-terminal flexibility allows HMW adiponectin to interact with diverse ligands, contributing to its functional versatility.