Abstract
An N-terminal region of the acid sphingomyelinase sequence (residues 89-165) is shown to be homologous to saposin-type sequences. By analogy with the known functions of saposins, this sphingomyelinase saposin-type domain may possess lipid-binding and/or sphingomyelinase-activator properties. This finding may prove to be important in the understanding of Niemann-Pick disease, which results from sphingomyelinase deficiency.
| Original language | English |
|---|---|
| Pages (from-to) | 359-61 |
| Number of pages | 3 |
| Journal | Protein Science |
| Volume | 3 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Feb 1994 |
Keywords
- Amino Acid Sequence
- Animals
- Entamoeba histolytica
- Glycoproteins
- Humans
- Molecular Sequence Data
- Saposins
- Sequence Alignment
- Sequence Homology, Amino Acid
- Sphingolipid Activator Proteins
- Sphingomyelin Phosphodiesterase