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

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)...

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Published inMolecular physics Vol. 111; no. 18-19; pp. 2865 - 2872
Main Authors Lovett, Janet E., Abbott, Rachel J.M., Roversi, Pietro, Caesar, Joseph J.E., Doria, Marianna, Jeschke, Gunnar, Timmel, Christiane R., Lea, Susan M.
Format Journal Article
LanguageEnglish
Published England Taylor & Francis 01.10.2013
Taylor & Francis Ltd
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Summary: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.
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Current address: Glycobiology Division, Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Current address: School of Cancer Sciences and MRC Centre for Immune Regulation, College of Medicine, University of Birmingham, Birmingham B15 2TT, UK.
ISSN:0026-8976
1362-3028
DOI:10.1080/00268976.2013.827754