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Molecular Aspects of C3 Interactions and Structural/Functional Analysis of C3 from Different Species

  • Conference paper
The Third Component of Complement

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 153))

Abstract

C3 plays a critical role in both pathways of complement activation due to its ability to bind to numerous other complement proteins. In addition, its interactions with several cell surface receptors make it a key participant in phagocytic and immunoregulatory processes. It is the purpose of this chapter to review the characteristics and unique structural features of human C3 which permit it to bind to various ligands and receptors. (For the purpose of this review, “ligands” of C3 are taken as those serum proteins which bind C3 and are distinguished from C3 receptors, which are cell surface proteins.) Here we also enunciate, from a structural viewpoint, our current knowledge of C3 from other species and discuss how their similarities, along with those of other homologous proteins, are used to further our understanding of the structure/function relationship of C3.

J.A. has an EMBO long-term fellowship (ALTF 298 — 1987). The Basel Institute for Immunology was founded by and is supported entirely by F. Hoffman — La Roche Ltd. Co., Basel, Switzerland.

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  1. Basel Institute for Immunology, Grenzacherstr. 487, 4005, Basel, Switzerland

    J. D. Becherer, J. Alsenz & J. D. Lambris

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  2. J. Alsenz
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    John D. Lambris Ph. D.

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Becherer, J.D., Alsenz, J., Lambris, J.D. (1990). Molecular Aspects of C3 Interactions and Structural/Functional Analysis of C3 from Different Species. In: Lambris, J.D. (eds) The Third Component of Complement. Current Topics in Microbiology and Immunology, vol 153. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-74977-3_3

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  • DOI: https://doi.org/10.1007/978-3-642-74977-3_3

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