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Evolution of lipoproteins deduced from protein sequence data.
1National Biomedical Research Foundation, Georgetown University Medical Center, Washington, D.C. 20007.
Summary
Human apolipoproteins A-I, C-I, C-III, and A-II share an 11-residue sequence pattern, suggesting common ancestry and evolutionary relationships across vertebrates and invertebrates.
Area of Science:
- Biochemistry
- Molecular Evolution
- Proteomics
Background:
- Human serum apolipoprotein A-I exhibits a distinct 11-residue sequence periodicity.
- This structural motif is also observed in other human apolipoproteins, including C-I, C-III, and A-II.
Purpose of the Study:
- To investigate the evolutionary origins of human apolipoproteins.
- To analyze sequence similarities and propose an evolutionary history for these proteins.
Main Methods:
- Computational analysis of apolipoprotein sequences.
- Comparative sequence analysis to identify conserved patterns.
Main Results:
- A conserved 11-residue sequence periodicity was identified across multiple human apolipoproteins.
- Computer analyses strongly support the hypothesis of a common ancestral origin for these proteins.
- An evolutionary history for these apolipoproteins is proposed based on sequence data.
Conclusions:
- The identified sequence patterns suggest a shared evolutionary path for human apolipoproteins.
- The estimated rate of protein change indicates their widespread presence in vertebrates.
- Related apolipoprotein structures are predicted to exist in invertebrates as well.