The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure
Lysosomal degradation of sphingolipids requires lipid-binding saposin proteins and hydrolytic enzymes. Here the authors present the crystal structure of the hydrolase β-galactocerebrosidase in complex with saposin SapA and give insights into the glycosphingolipid galactocerebroside degradation mecha...
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Format: | Article |
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Nature Portfolio
2018-01-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-02361-y |
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author | Chris H. Hill Georgia M. Cook Samantha J. Spratley Stuart Fawke Stephen C. Graham Janet E. Deane |
author_facet | Chris H. Hill Georgia M. Cook Samantha J. Spratley Stuart Fawke Stephen C. Graham Janet E. Deane |
author_sort | Chris H. Hill |
collection | DOAJ |
description | Lysosomal degradation of sphingolipids requires lipid-binding saposin proteins and hydrolytic enzymes. Here the authors present the crystal structure of the hydrolase β-galactocerebrosidase in complex with saposin SapA and give insights into the glycosphingolipid galactocerebroside degradation mechanism. |
first_indexed | 2024-12-18T04:39:23Z |
format | Article |
id | doaj.art-2892fdb00d5d43eb9babf8bf3fb7a3dc |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-18T04:39:23Z |
publishDate | 2018-01-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-2892fdb00d5d43eb9babf8bf3fb7a3dc2022-12-21T21:20:46ZengNature PortfolioNature Communications2041-17232018-01-01911910.1038/s41467-017-02361-yThe mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structureChris H. Hill0Georgia M. Cook1Samantha J. Spratley2Stuart Fawke3Stephen C. Graham4Janet E. Deane5Cambridge Institute for Medical Research, Department of Pathology, University of CambridgeCambridge Institute for Medical Research, Department of Pathology, University of CambridgeCambridge Institute for Medical Research, Department of Pathology, University of CambridgeCambridge Institute for Medical Research, Department of Pathology, University of CambridgeDepartment of Pathology, University of CambridgeCambridge Institute for Medical Research, Department of Pathology, University of CambridgeLysosomal degradation of sphingolipids requires lipid-binding saposin proteins and hydrolytic enzymes. Here the authors present the crystal structure of the hydrolase β-galactocerebrosidase in complex with saposin SapA and give insights into the glycosphingolipid galactocerebroside degradation mechanism.https://doi.org/10.1038/s41467-017-02361-y |
spellingShingle | Chris H. Hill Georgia M. Cook Samantha J. Spratley Stuart Fawke Stephen C. Graham Janet E. Deane The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure Nature Communications |
title | The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure |
title_full | The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure |
title_fullStr | The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure |
title_full_unstemmed | The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure |
title_short | The mechanism of glycosphingolipid degradation revealed by a GALC-SapA complex structure |
title_sort | mechanism of glycosphingolipid degradation revealed by a galc sapa complex structure |
url | https://doi.org/10.1038/s41467-017-02361-y |
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