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A structural basis for loop C-sheet polymerization in serpins.

Qingwei Zhang1, Ruby H P Law, Stephen P Bottomley

  • 1Department of Biochemistry and Molecular Biology, Monash University, Clayton, Melbourne, VIC 3800, Australia.

Journal of Molecular Biology
|February 1, 2008
PubMed
Summary
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The X-ray structure of bacterial tengpin revealed a latent conformation. This structure explains how serpins can form polymers, a process linked to diseases like dementia and thrombosis.

Area of Science:

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Serpins are proteins known to misfold and form polymers, contributing to various diseases.
  • Polymerization of serpins is implicated in conditions such as emphysema, thrombosis, and dementia.
  • While typically thought to polymerize via a loop A-sheet mechanism, latent serpins can also polymerize.

Purpose of the Study:

  • To determine the X-ray crystal structure of an N-terminally truncated bacterial serpin, tengpin (tengpinDelta42).
  • To elucidate the structural basis for polymerization in latent serpins.
  • To provide a potential mechanism for latent serpin polymerization.

Main Methods:

  • X-ray crystallography
  • Analysis of protein structure

Related Experiment Videos

  • Comparative structural analysis

    • Main Results:

    • The structure of tengpinDelta42 reveals a latent conformation with a hyperinserted reactive center loop.
    • The C beta-sheet remains exposed, facilitating interactions with neighboring molecules.
    • TengpinDelta42 forms a loop-C-sheet polymer in the crystal lattice.

    Conclusions:

    • The study provides a structural mechanism for polymerization by latent serpins.
    • This finding offers insights into the molecular basis of serpinopathies.
    • The observed polymerization mechanism may be relevant to diseases like familial encephalopathy with neuroserpin inclusion bodies.