C1q and tumor necrosis factor superfamily: modularity and versatility

C1q is the target recognition protein of the classical complement pathway and a major connecting link between innate and acquired immunity. As a charge pattern recognition molecule of innate immunity, C1q can engage a broad range of ligands via its globular (gC1q) domain and modulate immune cells, p...

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Bibliographic Details
Published in:Trends in immunology 2004-10, Vol.25 (10), p.551-561
Main Authors: Kishore, Uday, Gaboriaud, Christine, Waters, Patrick, Shrive, Annette K., Greenhough, Trevor J., Reid, Kenneth B.M., Sim, Robert B., Arlaud, Gerard J.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Angiogenesis
Animals
Apoptosis
Autoimmune diseases
Binding sites
Cell adhesion & migration
Cell growth
Collagen
Complement C1q - chemistry
Complement C1q - immunology
Evolution, Chemical
Homeostasis
Humans
Immune system
Ligands
Lymphocytes
Models, Molecular
Molecular Sequence Data
Peptides
Protein Structure, Quaternary
Proteins
Rodents
Sequence Homology, Amino Acid
Structural Homology, Protein
Structure-Activity Relationship
Tumor Necrosis Factor-alpha - chemistry
Tumor Necrosis Factor-alpha - immunology
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Summary:C1q is the target recognition protein of the classical complement pathway and a major connecting link between innate and acquired immunity. As a charge pattern recognition molecule of innate immunity, C1q can engage a broad range of ligands via its globular (gC1q) domain and modulate immune cells, probably via its collagen region. The gC1q signature domain, also found in many non-complement proteins, has a compact jelly-roll β-sandwich fold similar to that of the multifunctional tumor necrosis factor (TNF) ligand family. The members of this newly designated ‘C1q and TNF superfamily’ are involved in processes as diverse as host defense, inflammation, apoptosis, autoimmunity, cell differentiation, organogenesis, hibernation and insulin-resistant obesity. This review is an attempt to draw structural and functional parallels between the members of the C1q and TNF superfamily.
ISSN:1471-4906
1471-4981
DOI:10.1016/j.it.2004.08.006