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Structures of complement component C3 provide insights into the function and evolution of immunity

The mammalian complement system is a phylogenetically ancient cascade system that has a major role in innate and adaptive immunity. Activation of component C3 (1,641 residues) is central to the three complement pathways and results in inflammation and elimination of self and non-self targets. Here w... Full description

Journal Title: Nature (London) 2005, Vol.437 (7058), p.505-511
Main Author: Janssen, B.J.C
Other Authors: Huizinga, E.G , Raaijmakers, H.C.A , Roos, A , Daha, M.R , Nilsson-Ekdahl, K , Nilsson, B , Gros, P , Kristal- en structuurchemie , Crystal and Structural Chemistry 1 , Dep Scheikunde
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: London: Nature Publishing
ID: ISSN: 0028-0836
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recordid: cdi_swepub_primary_oai_DiVA_org_uu_25566
title: Structures of complement component C3 provide insights into the function and evolution of immunity
format: Article
creator:
  • Janssen, B.J.C
  • Huizinga, E.G
  • Raaijmakers, H.C.A
  • Roos, A
  • Daha, M.R
  • Nilsson-Ekdahl, K
  • Nilsson, B
  • Gros, P
  • Kristal- en structuurchemie
  • Crystal and Structural Chemistry 1
  • Dep Scheikunde
subjects:
  • Biological and medical sciences
  • Complement
  • Complement Activation
  • Complement C3 - chemistry
  • Complement C3 - immunology
  • Complement C3 - metabolism
  • Complement C3-C5 Convertases - metabolism
  • Complement C3/chemistry/immunology/metabolism
  • Complement C3c - chemistry
  • Complement C3c - metabolism
  • Complement C3c/chemistry/metabolism
  • Crystallography, X-Ray
  • Evolution, Molecular
  • Fundamental and applied biological sciences. Psychology
  • Fundamental immunology
  • Humans
  • International
  • Models, Biological
  • Models, Molecular
  • Molecular immunology
  • Protein Structure, Tertiary
ispartof: Nature (London), 2005, Vol.437 (7058), p.505-511
description: The mammalian complement system is a phylogenetically ancient cascade system that has a major role in innate and adaptive immunity. Activation of component C3 (1,641 residues) is central to the three complement pathways and results in inflammation and elimination of self and non-self targets. Here we present crystal structures of native C3 and its final major proteolytic fragment C3c. The structures reveal thirteen domains, nine of which were unpredicted, and suggest that the proteins of the alpha2-macroglobulin family evolved from a core of eight homologous domains. A double mechanism prevents hydrolysis of the thioester group, essential for covalent attachment of activated C3 to target surfaces. Marked conformational changes in the alpha-chain, including movement of a critical interaction site through a ring formed by the domains of the beta-chain, indicate an unprecedented, conformation-dependent mechanism of activation, regulation and biological function of C3.
language: eng
source:
identifier: ISSN: 0028-0836
fulltext: no_fulltext
issn:
  • 0028-0836
  • 1476-4687
  • 1476-4687
url: Link


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titleStructures of complement component C3 provide insights into the function and evolution of immunity
creatorJanssen, B.J.C ; Huizinga, E.G ; Raaijmakers, H.C.A ; Roos, A ; Daha, M.R ; Nilsson-Ekdahl, K ; Nilsson, B ; Gros, P ; Kristal- en structuurchemie ; Crystal and Structural Chemistry 1 ; Dep Scheikunde
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descriptionThe mammalian complement system is a phylogenetically ancient cascade system that has a major role in innate and adaptive immunity. Activation of component C3 (1,641 residues) is central to the three complement pathways and results in inflammation and elimination of self and non-self targets. Here we present crystal structures of native C3 and its final major proteolytic fragment C3c. The structures reveal thirteen domains, nine of which were unpredicted, and suggest that the proteins of the alpha2-macroglobulin family evolved from a core of eight homologous domains. A double mechanism prevents hydrolysis of the thioester group, essential for covalent attachment of activated C3 to target surfaces. Marked conformational changes in the alpha-chain, including movement of a critical interaction site through a ring formed by the domains of the beta-chain, indicate an unprecedented, conformation-dependent mechanism of activation, regulation and biological function of C3.
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subjectBiological and medical sciences ; Complement ; Complement Activation ; Complement C3 - chemistry ; Complement C3 - immunology ; Complement C3 - metabolism ; Complement C3-C5 Convertases - metabolism ; Complement C3/chemistry/immunology/metabolism ; Complement C3c - chemistry ; Complement C3c - metabolism ; Complement C3c/chemistry/metabolism ; Crystallography, X-Ray ; Evolution, Molecular ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; International ; Models, Biological ; Models, Molecular ; Molecular immunology ; Protein Structure, Tertiary
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descriptionThe mammalian complement system is a phylogenetically ancient cascade system that has a major role in innate and adaptive immunity. Activation of component C3 (1,641 residues) is central to the three complement pathways and results in inflammation and elimination of self and non-self targets. Here we present crystal structures of native C3 and its final major proteolytic fragment C3c. The structures reveal thirteen domains, nine of which were unpredicted, and suggest that the proteins of the alpha2-macroglobulin family evolved from a core of eight homologous domains. A double mechanism prevents hydrolysis of the thioester group, essential for covalent attachment of activated C3 to target surfaces. Marked conformational changes in the alpha-chain, including movement of a critical interaction site through a ring formed by the domains of the beta-chain, indicate an unprecedented, conformation-dependent mechanism of activation, regulation and biological function of C3.
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4Complement C3 - immunology
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titleStructures of complement component C3 provide insights into the function and evolution of immunity
authorJanssen, B.J.C ; Huizinga, E.G ; Raaijmakers, H.C.A ; Roos, A ; Daha, M.R ; Nilsson-Ekdahl, K ; Nilsson, B ; Gros, P ; Kristal- en structuurchemie ; Crystal and Structural Chemistry 1 ; Dep Scheikunde
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6Complement C3-C5 Convertases - metabolism
7Complement C3/chemistry/immunology/metabolism
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13Fundamental and applied biological sciences. Psychology
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15Humans
16International
17Models, Biological
18Models, Molecular
19Molecular immunology
20Protein Structure, Tertiary
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abstractThe mammalian complement system is a phylogenetically ancient cascade system that has a major role in innate and adaptive immunity. Activation of component C3 (1,641 residues) is central to the three complement pathways and results in inflammation and elimination of self and non-self targets. Here we present crystal structures of native C3 and its final major proteolytic fragment C3c. The structures reveal thirteen domains, nine of which were unpredicted, and suggest that the proteins of the alpha2-macroglobulin family evolved from a core of eight homologous domains. A double mechanism prevents hydrolysis of the thioester group, essential for covalent attachment of activated C3 to target surfaces. Marked conformational changes in the alpha-chain, including movement of a critical interaction site through a ring formed by the domains of the beta-chain, indicate an unprecedented, conformation-dependent mechanism of activation, regulation and biological function of C3.
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