Structure, function and molecular genetics of human and murine C1r
| Autor: | Christine Gaboriaud, Gérard Garnier, Juan C. Fontecilla-Camps, Nicole M. Thielens, Monika Budayova-Spano, John E. Volanakis, Gérard J. Arlaud, Antonella Circolo |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
medicine.medical_specialty
Proteases Immunology Protein Structure Secondary Serine Enzyme activator Mice Structure-Activity Relationship Protein structure Molecular genetics medicine Immunology and Allergy Structure–activity relationship Animals Humans Protein Isoforms Complement Pathway Classical Serine protease biology Complement C1s Complement C1r Hematology Cell biology Complement system Enzyme Activation biology.protein |
| Zdroj: | Immunobiology. 205(4-5) |
| ISSN: | 0171-2985 |
| Popis: | C1r, the enzyme responsible for intrinsic activation of the C1 complex of complement, is a modular serine protease featuring an overall structural organization homologous to those of C1s and the mannan-binding lectin-associated serine proteases (MASPs). This review will initially summarize current information on the structure and function of C1r, with particular emphasis on the three-dimensional structure of its catalytic domain, which provides new insights into the activation mechanism of C1. The second part of this review will focus on recent discoveries dealing with a truncated, C1r-related protein, and the occurrence in the mouse of two isoforms, C1rA and C1rB, exhibiting tissue-specific expression patterns. |
| Databáze: | OpenAIRE |
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