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


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.

SUBMITTER: Lovett JE 

PROVIDER: S-EPMC4056885 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature

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

Lovett Janet E JE   Abbott Rachel J M RJ   Roversi Pietro P   Johnson Steven S   Caesar Joseph J E JJ   Doria Marianna M   Jeschke Gunnar G   Timmel Christiane R CR   Lea Susan M SM  

Molecular physics 20131009 18-19


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 mod  ...[more]

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