Article
Structural features in the NH2-terminal region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase.
The Journal of biological chemistry - 5 Oct 1990
Nothwehr S F, Gordon J I
Abstract excerpt
The 20-amino acid signal peptide of human pre (delta pro)apolipoprotein A-II contains the tripartite domain structure typical of eukaryotic prepeptides, i.e. a positively charged NH2-terminal (n) region, a hydrophobic core (h) region, and a COOH-terminal polar domain (c region). This signal sequence has multiple potential sites for cotranslational processing making it an attractive model for assessing the...
Topics
- Amino Acid Sequence
- Apolipoprotein A-II
- Apolipoproteins A
- Base Sequence
- Endopeptidases
- Humans
- Lipoproteins, HDL
- Membrane Proteins
- Molecular Sequence Data
- Mutation
- Oligonucleotide Probes