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Science 332 (6029): 608-611

Copyright © 2011 by the American Association for the Advancement of Science

A Crystal Structure of the Complex Between Human Complement Receptor 2 and Its Ligand C3d

Jean M. H. van den Elsen1,*, and David E. Isenman2,*

Abstract: The interaction of complement receptor 2 (CR2)—which is present on B cells and follicular dendritic cells—with its antigen-bound ligand C3d results in an enhanced antibody response, thus providing an important link between the innate and adaptive immune systems. Although a cocrystal structure of a complex between C3d and the ligand-binding domains of CR2 has been published, several aspects of this structure, including the position in C3d of the binding interface, remained controversial because of disagreement with biochemical data. We now report a cocrystal structure of a CR2(SCR1-2):C3d complex at 3.2 angstrom resolution in which the interaction interfaces differ markedly from the previously published structure and are consistent with the biochemical data. It is likely that, in the previous structure, the interaction was influenced by the presence of zinc acetate additive in the crystallization buffer, leading to a nonphysiological complex. Detailed knowledge of the binding interface now at hand gives the potential to exploit the interaction in vaccine design or in therapeutics directed against autoreactive B cells.

1 Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK.
2 Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.

* To whom correspondence should be addressed. E-mail: d.isenman{at}utoronto.ca (D.E.I.); bssjmhve{at}bath.ac.uk (J.M.H.v.d.E.)

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Unique structure of iC3b resolved at a resolution of 24 A by 3D-electron microscopy.
M. Alcorlo, R. Martinez-Barricarte, F. J. Fernandez, C. Rodriguez-Gallego, A. Round, M. C. Vega, C. L. Harris, S. R. de Cordoba, and O. Llorca (2011)
PNAS 108, 13236-13240
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