Protein Sci. 1994 Feb;3(2):359-61.

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

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Department 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.

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PMCID:: PMC2142785

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