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

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)359-61
Number of pages3
JournalProtein Science
Volume3
Issue number2
DOIs
Publication statusPublished - 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

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