Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 100, Issue 1, Pages 38-43Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0136947100
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- NCRR NIH HHS [P41 RR001646] Funding Source: Medline
- NINDS NIH HHS [NS31271] Funding Source: Medline
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Saposin B is a small, nonenzymatic glycosphingolipid activator protein required for the breakdown of cerebroside sulfates (sulfatides) within the lysosome. The protein can extract target lipids from membranes, forming soluble protein-lipid complexes that are recognized by arylsulfatase A. The crystal structure of human saposin B reveals an unusual shell-like dimer consisting of a monolayer of alpha-helices enclosing a large hydrophobic cavity. Although the secondary structure of saposin B is similar to that of the known monomeric members of the saposin-like superfamily, the helices are repacked into a different tertiary arrangement to form the homodimer. A comparison of the two forms of the saposin B dinner suggests that extraction of target lipids from membranes involves a conformational change that facilitates access to the inner cavity.
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