Investigating the structure of the factor B vWF-A domain/CD55 protein-protein complex using DEER spectroscopy: successes and pitfalls

Janet E. Lovett*, Rachel J. M. Abbott, Pietro Roversi, Steven Johnson, Joseph J. E. Caesar, Marianna Doria, Gunnar Jeschke, Christiane R. Timmel, Susan M. Lea

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

The electron paramagnetic resonance technique of double electron-electron resonance (DEER) was used to measure nanometre-scale distances between nitroxide spin labels attached to the complement regulatory protein CD55 (also known as decay accelerating factor) and the von Willebrand factor A (vWF-A) domain of factor B. Following a thorough assessment of the quality of the data, distances obtained from good-quality measurements are compared to predicted distances from a previously hypothesised model for the complex and are found to be incompatible. The success of using these distances as restraints in multi-body docking routines is presented critically.

Original languageEnglish
Pages (from-to)2865-2872
Number of pages8
JournalMolecular Physics
Volume111
Issue number18-19
DOIs
Publication statusPublished - 1 Oct 2013

Keywords

  • DEER
  • distance restraints
  • CD55
  • vWF-A
  • decay acceleration
  • DECAY-ACCELERATING FACTOR
  • PATHWAY C3 CONVERTASE
  • DISTANCE MEASUREMENTS
  • ALTERNATIVE PATHWAY
  • ESCHERICHIA-COLI
  • EPR SPECTROSCOPY
  • NMR SYSTEM
  • REFINEMENT
  • MODEL
  • BIOMACROMOLECULES

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