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Structure of C3b reveals conformational changes that underlie complement activity

Author

Listed:
  • Bert J. C. Janssen

    (Utrecht University)

  • Agni Christodoulidou

    (University of Pennsylvania)

  • Andrew McCarthy

    (Grenoble Outstation)

  • John D. Lambris

    (University of Pennsylvania)

  • Piet Gros

    (Utrecht University)

Abstract

Fishing for complement Three papers in this issue report the first X-ray structures of C3b, the active form of human complement C3. The complement system is a family of blood serum proteins and cell-surface receptors that recognizes pathogens and unleashes the immune response against them. The powerhouse of the C3 protein is a thioester group: when activated it binds to an acceptor on the pathogen and marks it for destruction. There are similar thioesters in host cells too, so the C3 thioester has to be kept tightly under wraps. Knowledge of the structure of the active form of C3b is a step towards designing therapies to manipulate the complement system. Inappropriate activation of the complement system has been implicated in various diseases including arthritis, asthma, lupus erythematosus, autoimmune heart disease and multiple sclerosis.

Suggested Citation

  • Bert J. C. Janssen & Agni Christodoulidou & Andrew McCarthy & John D. Lambris & Piet Gros, 2006. "Structure of C3b reveals conformational changes that underlie complement activity," Nature, Nature, vol. 444(7116), pages 213-216, November.
    • Handle: RePEc:nat:nature:v:444:y:2006:i:7116:d:10.1038_nature05172
    DOI: 10.1038/nature05172
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    Cited by:

    1. Nadia Sukusu Nielsen & Alessandra Zarantonello & Seandean Lykke Harwood & Kathrine Tejlgård Jensen & Katarzyna Kjøge & Ida B. Thøgersen & Leif Schauser & Jesper Lykkegaard Karlsen & Gregers R. Anderse, 2022. "Cryo-EM structures of human A2ML1 elucidate the protease-inhibitory mechanism of the A2M family," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Christina Lamers & Xiaoguang Xue & Martin Smieško & Henri Son & Bea Wagner & Nadja Berger & Georgia Sfyroera & Piet Gros & John D. Lambris & Daniel Ricklin, 2022. "Insight into mode-of-action and structural determinants of the compstatin family of clinical complement inhibitors," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. Francisco J. Fernández & Jorge Santos-López & Rubén Martínez-Barricarte & Javier Querol-García & Héctor Martín-Merinero & Sergio Navas-Yuste & Martin Savko & William E. Shepard & Santiago Rodríguez de, 2022. "The crystal structure of iC3b-CR3 αI reveals a modular recognition of the main opsonin iC3b by the CR3 integrin receptor," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    4. Hagen Sülzen & Jakub Began & Arun Dhillon & Sami Kereïche & Petr Pompach & Jitka Votrubova & Farnaz Zahedifard & Adriana Šubrtova & Marie Šafner & Martin Hubalek & Maaike Thompson & Martin Zoltner & S, 2023. "Cryo-EM structures of Trypanosoma brucei gambiense ISG65 with human complement C3 and C3b and their roles in alternative pathway restriction," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    5. Sara T Ibrahim & Rajkumar Chinnadurai & Ibrahim Ali & Debbie Payne & Gillian I Rice & William G Newman & Eman Algohary & Ahmed G Adam & Philip A Kalra, 2020. "Genetic polymorphism in C3 is associated with progression in chronic kidney disease (CKD) patients with IgA nephropathy but not in other causes of CKD," PLOS ONE, Public Library of Science, vol. 15(1), pages 1-16, January.

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