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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Bibliographic Details
Published in:Molecular physics 2013-10, Vol.111 (18-19), p.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: Article
Language:English
Subjects:
Assessments
CD55
decay acceleration
DEER
distance restraints
Invited
Proteins
Spectrum analysis
vWF-A
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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.
ISSN:0026-8976
1362-3028
DOI:10.1080/00268976.2013.827754