Crystal structure of saposin B reveals a dimeric shell for lipid binding
| dc.contributor.author | Ahn, Victoria E. | |
| dc.contributor.author | Faull, Kym F. | |
| dc.contributor.author | Whitelegge, Julian P. | |
| dc.date.accessioned | 2021-09-30T10:49:47Z | |
| dc.date.available | 2021-09-30T10:49:47Z | |
| dc.date.issued | 2003 | |
| dc.description.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 -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. | en_US |
| dc.identifier.citation | hn, V. E. et al. (2003). Crystal structure of saposin B reveals a dimeric shell for lipid binding. Proceedings of the National Academy of Sciences of the United States of America, 100(1), 38–43. https://doi.org/10.1073/pnas.0136947100 | en_US |
| dc.identifier.issn | 1091-6490 | |
| dc.identifier.uri | http://hdl.handle.net/10566/6842 | |
| dc.language.iso | en | en_US |
| dc.publisher | National Academy of Sciences | en_US |
| dc.subject | Chemistry | en_US |
| dc.subject | Lipid binding | en_US |
| dc.subject | Protein | en_US |
| dc.subject | Saposin B | en_US |
| dc.title | Crystal structure of saposin B reveals a dimeric shell for lipid binding | en_US |
| dc.type | Article | en_US |