Related Experiment Videos
Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence
C M Mackinnon1, P E Carter, S J Smyth
1Department of Biochemistry, University of Aberdeen, Scotland.
European Journal of Biochemistry
|December 15, 1987
Summary
The complete amino acid sequence of human complement component C1s was determined using cDNA sequencing. This reveals its domain structure, including homology to C1r and other proteins.
Area of Science:
- Immunology
- Molecular Biology
- Biochemistry
Background:
- Human complement component C1s is a crucial part of the classical complement pathway.
- Understanding its structure is essential for elucidating complement system function.
Purpose of the Study:
- To determine the complete amino acid sequence of human complement component C1s.
- To analyze the domain structure and homologies of C1s.
Main Methods:
- Nucleotide sequencing of cDNA clones from a human liver library.
- Probing with synthetic oligonucleotides.
- Validation with independent amino acid sequence data.
Main Results:
- The full amino acid sequence (673 residues + 15 leader residues) of human C1s was elucidated.
- The N-terminal region (422 residues) exhibits five domains with homologies to C1r and epidermal growth factor.
- The C-terminal region (251 residues) confirms the serine protease domain.
Conclusions:
- The determined sequence provides a comprehensive understanding of human C1s structure.
- Identified homologies offer insights into the evolution and function of complement proteins.