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Crystal structure of saposin B reveals a dimeric shell for lipid binding

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Ahn, Victoria E., Faull, Kym F., Whitelegge, Julian P., Fluharty, Arvan L., Privé, Gilbert G.·2003·Proceedings of the National Academy of Sciences

Abstract

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 α-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 dimer suggests that extraction of target lipids from membranes involves a conformational change that facilitates access to the inner cavity.

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Metadata

Authors
Ahn, V. E., Faull, K. F., Whitelegge, J. P., Fluharty, A. L., & Privé, G. G.
Venue
Proceedings of the National Academy of Sciences
Published
2002-12-23
Volume
100
Issue
1
Pages
38-43
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2041844634
Cited by
182
References
0
FWCI
6.61
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Crystal structure of saposin B reveals a dimeric shell for lipid binding. https://app.cochat.ai/papers/10.1073/pnas.0136947100
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Ahn, V. E., Faull, K. F., Whitelegge, J. P., Fluharty, A. L., & Privé, G. G. (2003). Crystal structure of saposin B reveals a dimeric shell for lipid binding. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0136947100

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