Format

Send to:

Choose Destination
See comment in PubMed Commons below
Protein Sci. 1994 Feb;3(2):359-61.

Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D.

Author information

  • 1Department of Biochemistry, University of Oxford, United Kingdom.

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.

PMID:
8003971
[PubMed - indexed for MEDLINE]
PMCID:
PMC2142785
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for John Wiley & Sons, Inc. Icon for PubMed Central
    Loading ...
    Write to the Help Desk