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Related Experiment Videos

Structure of cardiac gap junction intercellular channels

M Yeager1

  • 1Department of Cell Biology, Scripps Research Institute, La Jolla, California 92037, USA.

Journal of Structural Biology
|June 6, 1998
PubMed
Summary
This summary is machine-generated.

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Connexins form gap junctions, crucial for heart cell communication and synchronized contraction. Structural analysis reveals alpha-helices in connexin channels, explaining stable electrical seals for cardiac conduction.

Area of Science:

  • Structural biology
  • Molecular biophysics
  • Cardiovascular science

Background:

  • Gap junction proteins, connexins, are polytopic membrane channels essential for intercellular communication.
  • Alpha 1 connexin (Cx43) is the primary gap junction protein in the heart, mediating synchronized cardiac contraction.
  • Connexin channels form through docked connexons, each composed of six connexin subunits.

Purpose of the Study:

  • To elucidate the structural basis of connexin channel function in cardiac conduction.
  • To analyze the quaternary arrangement of connexin subunits within the channel.

Main Methods:

  • Two-dimensional crystallization of a recombinant C-terminal truncation mutant of alpha 1 connexin (alpha 1Cx263T).
  • High-resolution (better than 7 A) electron cryocrystallography.

Related Experiment Videos

  • Analysis of projection density maps to determine channel structure.

    • Main Results:

    • The intercellular channel is lined by two rings of six alpha-helices each.
    • One ring is within the channel lumen, and the other interfaces with membrane lipids.
    • These alpha-helical rings are staggered by 30 degrees, predicting a 30-degree stagger between docked connexons.

    Conclusions:

    • The staggered arrangement of connexons, where each subunit interacts with two in the apposed connexon, likely confers stability.
    • This structural feature ensures a tight electrical seal for efficient intercellular current flow during cardiac conduction.