The control protein Factor H (FH) is a crucial regulator of the innate immune complement system, where it is active on host cell membranes and in the fluid phase. Mutations impairing the binding capacity of FH lead to severe autoimmune diseases. Here, we studied the solution structure of full-length FH, in its free state and bound to the C3b complement protein. To do so, we used two powerful techniques, hydroxyl radical protein footprinting (HRPF) and chemical cross-linking coupled with mass spectrometry (MS), to probe the structural rearrangements and to identify protein interfaces. The footprint of C3b on the FH surface matches existing crystal structures of C3b complexed with the N- and C-terminal fragments of FH. In addition, we revealed the position of the central portion of FH in the protein complex. Moreover, cross-linking studies confirmed the involvement of the C-terminus in the dimerization of FH.
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K-Ras4B membrane-anchored dimers in the cell. Dimerization can take place through helical (left) and beta-sheet (right) interfaces. The major (front) and minor (back) conformations are shown. For further details please see pp. 1719–1732. Image kindly provided by Ruth Nussinov. - PDF Icon PDF LinkFront Matter
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Research Article|
June 10 2016
Probing the solution structure of Factor H using hydroxyl radical protein footprinting and cross-linking
Anna Baud;
Anna Baud
*CNRS, UMR8587, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
†Université Evry-Val-d'Essonne, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
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Florence Gonnet;
Florence Gonnet
*CNRS, UMR8587, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
†Université Evry-Val-d'Essonne, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
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Isabelle Salard;
Isabelle Salard
*CNRS, UMR8587, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
†Université Evry-Val-d'Essonne, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
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Maxime Le Mignon;
Maxime Le Mignon
*CNRS, UMR8587, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
†Université Evry-Val-d'Essonne, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
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Alexandre Giuliani;
Alexandre Giuliani
‡Synchrotron Soleil, BP 48, 91192 Gif-sur-Yvette Cedex, France
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Pascal Mercère;
Pascal Mercère
‡Synchrotron Soleil, BP 48, 91192 Gif-sur-Yvette Cedex, France
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Bianca Sclavi;
Bianca Sclavi
§CNRS, UMR 8113, LBPA, ENS Cachan, Cachan 94235, France
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Régis Daniel
Régis Daniel
1
*CNRS, UMR8587, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
†Université Evry-Val-d'Essonne, Laboratoire Analyse et Modélisation pour la Biologie et l'Environnement, 91025 Evry, France
1To whom correspondence should be addressed (email regis.daniel@univ-evry.fr).
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Publisher: Portland Press Ltd
Received:
March 15 2016
Revision Received:
April 07 2016
Accepted:
April 19 2016
Accepted Manuscript online:
April 20 2016
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2016 The Author(s). published by Portland Press Limited on behalf of the Biochemical Society
2016
Biochem J (2016) 473 (12): 1805–1819.
Article history
Received:
March 15 2016
Revision Received:
April 07 2016
Accepted:
April 19 2016
Accepted Manuscript online:
April 20 2016
Citation
Anna Baud, Florence Gonnet, Isabelle Salard, Maxime Le Mignon, Alexandre Giuliani, Pascal Mercère, Bianca Sclavi, Régis Daniel; Probing the solution structure of Factor H using hydroxyl radical protein footprinting and cross-linking. Biochem J 15 June 2016; 473 (12): 1805–1819. doi: https://doi.org/10.1042/BCJ20160225
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