Structural insight on the recognition of surface-bound opsonins by the integrin I domain of complement receptor 3

Bajic, Goran, Yatime, Laure, Sim, Robert B., Vorup-Jensen, Thomas and Andersen, Gregers R. (2013) Structural insight on the recognition of surface-bound opsonins by the integrin I domain of complement receptor 3. Proceedings of the National Academy of Sciences of the United States of America (PNAS) ISSN 1091-6490, 110(41), pp. 16426-16431. ISSN (print) 0027-8424

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Abstract

Complement receptors (CRs), expressed notably on myeloid and lymphoid cells, play an essential function in the elimination of complement-opsonized pathogens and apoptotic/necrotic cells. In addition, these receptors are crucial for the cross-talk between the innate and adaptive branches of the immune system. CR3 (also known as Mac-1, integrin αMβ2, or CD11b/CD18) is expressed on all macrophages and recognizes iC3b on complement-opsonized objects, enabling their phagocytosis. We demonstrate that the C3d moiety of iC3b harbors the binding site for the CR3 αI domain, and our structure of the C3d:αI domain complex rationalizes the CR3 selectivity for iC3b. Based on extensive structural analysis, we suggest that the choice between a ligand glutamate or aspartate for coordination of a receptor metal ion-dependent adhesion site-bound metal ion is governed by the secondary structure of the ligand. Comparison of our structure to the CR2:C3d complex and the in vitro formation of a stable CR3:C3d:CR2 complex suggests a molecular mechanism for the hand-over of CR3-bound immune complexes from macrophages to CR2-presenting cells in lymph nodes.

Item Type: Article
Research Area: Allied health professions and studies
Faculty, School or Research Centre: Faculty of Science, Engineering and Computing (until 2017)
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Depositing User: Susan Miles
Date Deposited: 15 Nov 2013 14:26
Last Modified: 17 Mar 2014 09:37
DOI: https://doi.org/10.1073/pnas.1311261110
URI: http://eprints.kingston.ac.uk/id/eprint/26803

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