Structured Summary
Abstract
A 80-kDa subcomponent of complement C1, existing as a SERINE PROTEASE proenzyme in the intact complement C1 complex. When COMPLEMENT C1Q is bound to antibodies, the changed tertiary structure causes autolytic activation of complement C1r which is cleaved into two chains, A (heavy) and B (light, the serine protease), connected by disulfide bonds. The activated C1r serine protease, in turn, activates COMPLEMENT C1S proenzyme by cleaving the Arg426-Ile427 bond. No fragment is released when either C1r or C1s is cleaved.
MeSH Record
Classification
Broader headings
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Drug Class
Pharmacological Action
MeSH Record
Synonyms
6 entry terms
- C1r Complement
- Complement 1r
- Complement Component 1r
- C1r, Complement
- Complement, C1r
- Component 1r, Complement
MeSH Record
Aspects Covered
29 allowable subheadings
Indexed with the subheadings administration & dosage, adverse effects, agonists, analysis, antagonists & inhibitors, biosynthesis, cerebrospinal fluid, chemical synthesis, chemistry, classification, deficiency, drug effects, economics, genetics, history, immunology, isolation & purification, metabolism, pharmacokinetics, pharmacology, physiology, poisoning, radiation effects, standards, supply & distribution, therapeutic use, toxicity, ultrastructure, urine.
MeSH Record
History Note
2006 (1990)
MeSH Record
Previous Indexing
- Complement 1 (1979-1989)
- Complement Activating Enzymes (1979-1989)
- Enzyme Precursors (1979-1982)
MeSH Hierarchy
Tree Numbers
AMA Style
References
- National Library of Medicine. Complement C1r. Medical Subject Headings (MeSH). 2026. Unique ID D015923. http://id.nlm.nih.gov/mesh/2026/D015923
- Complement C1r. In: Wikidata. https://www.wikidata.org/wiki/Q21111742