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Related Experiment Videos

How does a topological inversion change the evolutionary constraints on membrane proteins?

Hisako Ichihara1, Hiromi Daiyasu, Hiroyuki Toh

  • 1Bioinformatics Center, Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.

Protein Engineering, Design & Selection : PEDS
|April 7, 2004
PubMed
Summary

Aquaporin and ClC channel proteins have N- and C-terminal domains with opposite membrane orientations. Different evolutionary pressures on these domains influence protein structure, particularly on the channel pore surface.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Evolutionary Biology

Background:

  • Aquaporin and ClC channel proteins feature two-fold tandem repeats with opposing N- and C-terminal domain orientations.
  • Extracellular and cytoplasmic environments impose distinct evolutionary constraints, such as the positive-inside rule, on membrane proteins.

Purpose of the Study:

  • To investigate if differing evolutionary constraints on extracellular and cytoplasmic sides affect the N- and C-terminal domains of aquaporin and ClC channel proteins.
  • To analyze the impact of topological inversion on protein evolution and structure.

Main Methods:

  • Alignment of N- and C-terminal domains of aquaporin and ClC channel proteins.
  • Calculation of residue composition and conservation differences between domains using multiple methods.

Related Experiment Videos

  • Mapping of significantly differing residues onto the tertiary protein structure.

    • Main Results:

    • Residues showing significant differences between domains predominantly clustered on the channel pore surface.
    • A small number of differing residues were mapped to the extracellular or cytoplasmic sides.
    • Method refinement enhanced detection of sites related to the positive-inside rule.

    Conclusions:

    • The findings support the hypothesis that topological inversion between N- and C-terminal domains correlates with distinct evolutionary constraints.
    • Evolutionary pressures differentially shape protein regions exposed to different cellular environments, particularly impacting the channel pore.