Format

Send to

Choose Destination
See comment in PubMed Commons below
Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):589-94. doi: 10.1107/S0907444908003120. Epub 2008 Apr 19.

Structures of the human ceramide activator protein saposin D.

Author information

1
Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.

Abstract

Saposin D is a sphingolipid activator protein required for the lysosomal breakdown of ceramide to a fatty acid and sphingosine by acid ceramidase. The crystal structure of saposin D has been determined in two different crystal forms, resulting in a total of six crystallographically independent views of this small 80-amino-acid protein. All of the structures are highly similar and reveal the monomeric form of the saposin fold previously seen in the crystal structures of saposins A and C. Saposin D is slightly more compact than the related saposins A and C owing to a slight repositioning of the 'stem' and 'hairpin' regions of the protein.

PMID:
18453694
DOI:
10.1107/S0907444908003120
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for International Union of Crystallography
    Loading ...
    Support Center