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 in | Molecular physics Vol. 111; no. 18-19; pp. 2865 - 2872 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Taylor & Francis
01.10.2013
Taylor & Francis Ltd |
Subjects | |
Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 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 |