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Related Experiment Videos

Three-dimensional structure of a complement control protein module in solution.

D G Norman1, P N Barlow, M Baron

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

Journal of Molecular Biology
|June 20, 1991
PubMed
Summary
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Complement control protein (CCP) modules, crucial in the complement system, adopt a conserved beta-sandwich structure. This structural determination aids in understanding CCP protein family variations and potential disulfide bridge accommodation.

Area of Science:

  • Structural Biology
  • Immunology
  • Biochemistry

Background:

  • Complement control protein (CCP) modules, also known as short consensus repeats, are prevalent in numerous proteins, particularly within the complement system.
  • Over 140 CCP modules have been identified across more than 20 proteins, highlighting their functional significance.
  • Understanding the three-dimensional structure of CCP modules is essential for elucidating their role in biological processes.

Purpose of the Study:

  • To determine the solution structure of the 16th CCP module from human complement factor H.
  • To provide a structural basis for understanding the conservation and variation within CCP module families.
  • To investigate the structural implications of sequence variations, including extra cysteine residues.

Main Methods:

Related Experiment Videos

  • Utilized 2-dimensional nuclear magnetic resonance (2D NMR) spectroscopy.
  • Employed restrained simulated annealing protocols incorporating distance and angle restraints derived from NMR data.
  • Analyzed sequence alignments in conjunction with the determined 3D structure.

Main Results:

  • The CCP module adopts a conserved beta-sandwich fold, characterized by specific beta-strand arrangements and a compact hydrophobic core.
  • Structural analysis revealed high conservation in structurally important residues, with variations primarily located in loop regions.
  • The determined model accommodates extra cysteine residues, suggesting flexibility for disulfide bridge formation.

Conclusions:

  • The determined beta-sandwich structure serves as an accurate model for other CCP modules.
  • Structural conservation and the localization of sequence variations in loops explain functional and evolutionary aspects of CCP modules.
  • The structural framework supports the potential for disulfide bridge formation in certain CCP families.