Edinburgh Research Explorer

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

Research output: Contribution to journalArticle

  • 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

Related Edinburgh Organisations

Original languageEnglish
Pages (from-to)2865-2872
Number of pages8
JournalMolecular Physics
Volume111
Issue number18-19
DOIs
Publication statusPublished - 9 Oct 2013

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.

    Research areas

  • 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

ID: 14127180