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Related Experiment Videos

Solution structure of a pair of complement modules by nuclear magnetic resonance

P N Barlow1, A Steinkasserer, D G Norman

  • 1Department of Biochemistry, University of Oxford, U.K.

Journal of Molecular Biology
|July 5, 1993
PubMed
Summary
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Researchers studied human complement factor H modules H15 and H16, finding they fold independently and exhibit flexibility. This structural insight helps understand the overall factor H protein and its role in complement control.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • Human complement factor H regulates the complement system.
  • It comprises 20 complement control (C-) modules.
  • Understanding module interactions is key to factor H function.

Purpose of the Study:

  • To determine the solution structure of human complement factor H modules H15 and H16.
  • To investigate the structural relationship and flexibility between adjacent modules.
  • To assess autonomous folding of individual modules within factor H.

Main Methods:

  • Expression of human complement factor H H15-16 in a yeast vector.
  • Structure determination using two-dimensional 1H-NMR.
  • Analysis of nuclear Overhauser effects to map intermodular interactions.

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Main Results:

  • H15 and H16 structures are similar to previously determined modules, suggesting a common topology for C-modules.
  • Tertiary structures of H15 and H16 are conserved whether expressed individually or paired.
  • A small intermodular interface exists, with significant flexibility in the 'twist' angle between modules.

Conclusions:

  • Individual complement control modules of factor H appear to fold autonomously.
  • The H15-16 pair exhibits relative flexibility, particularly in rotational freedom.
  • These findings inform models of the intact factor H protein structure and function.