Structural characteristics around O-glycosylation sites in mammalian proteins
The structural characteristic that O-glycan sugars prefer to bind to the regions forming β-strand structures is reported in this paper. While N-acetylglucosamine (GlcNAc) and mannose (Man) modification sites were contained in β-strand structures, fucose (Fuc) modification sites were found on β-stran...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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The Japan Society of Mechanical Engineers
2014-10-01
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| Series: | Journal of Biomechanical Science and Engineering |
| Subjects: | |
| Online Access: | https://www.jstage.jst.go.jp/article/jbse/10/1/10_14-00249/_pdf/-char/en |
| _version_ | 1811292393782116352 |
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| author | Kenji ETCHUYA Yuri MUKAI |
| author_facet | Kenji ETCHUYA Yuri MUKAI |
| author_sort | Kenji ETCHUYA |
| collection | DOAJ |
| description | The structural characteristic that O-glycan sugars prefer to bind to the regions forming β-strand structures is reported in this paper. While N-acetylglucosamine (GlcNAc) and mannose (Man) modification sites were contained in β-strand structures, fucose (Fuc) modification sites were found on β-strand and coil structures close to the β-strand structures. In particular, most Fuc modifications in EGF-like domains were identified on the edge of β-strand structures. Glycosyltransferases is thought to recognize motif residues in β-strand structures. The finding in this study that O-glycosylation preferred β-conformation and coil structures can be applied for the development of prediction methods and be useful to improve prediction accuracy. |
| first_indexed | 2024-04-13T04:44:47Z |
| format | Article |
| id | doaj.art-043aacebb12e4576a73dd7247d2d12fb |
| institution | Directory Open Access Journal |
| issn | 1880-9863 |
| language | English |
| last_indexed | 2024-04-13T04:44:47Z |
| publishDate | 2014-10-01 |
| publisher | The Japan Society of Mechanical Engineers |
| record_format | Article |
| series | Journal of Biomechanical Science and Engineering |
| spelling | doaj.art-043aacebb12e4576a73dd7247d2d12fb2022-12-22T03:01:52ZengThe Japan Society of Mechanical EngineersJournal of Biomechanical Science and Engineering1880-98632014-10-0110114-0024914-0024910.1299/jbse.14-00249jbseStructural characteristics around O-glycosylation sites in mammalian proteinsKenji ETCHUYA0Yuri MUKAI1Department of Electronics, Graduate School of Science and Technology, Meiji UniversityDepartment of Electronics and Bioinfomatics, School of Science and Technology, Meiji UniversityThe structural characteristic that O-glycan sugars prefer to bind to the regions forming β-strand structures is reported in this paper. While N-acetylglucosamine (GlcNAc) and mannose (Man) modification sites were contained in β-strand structures, fucose (Fuc) modification sites were found on β-strand and coil structures close to the β-strand structures. In particular, most Fuc modifications in EGF-like domains were identified on the edge of β-strand structures. Glycosyltransferases is thought to recognize motif residues in β-strand structures. The finding in this study that O-glycosylation preferred β-conformation and coil structures can be applied for the development of prediction methods and be useful to improve prediction accuracy.https://www.jstage.jst.go.jp/article/jbse/10/1/10_14-00249/_pdf/-char/enbioinformaticso-glycosylationpost-translational modificationsecondary structuremammalian protein |
| spellingShingle | Kenji ETCHUYA Yuri MUKAI Structural characteristics around O-glycosylation sites in mammalian proteins Journal of Biomechanical Science and Engineering bioinformatics o-glycosylation post-translational modification secondary structure mammalian protein |
| title | Structural characteristics around O-glycosylation sites in mammalian proteins |
| title_full | Structural characteristics around O-glycosylation sites in mammalian proteins |
| title_fullStr | Structural characteristics around O-glycosylation sites in mammalian proteins |
| title_full_unstemmed | Structural characteristics around O-glycosylation sites in mammalian proteins |
| title_short | Structural characteristics around O-glycosylation sites in mammalian proteins |
| title_sort | structural characteristics around o glycosylation sites in mammalian proteins |
| topic | bioinformatics o-glycosylation post-translational modification secondary structure mammalian protein |
| url | https://www.jstage.jst.go.jp/article/jbse/10/1/10_14-00249/_pdf/-char/en |
| work_keys_str_mv | AT kenjietchuya structuralcharacteristicsaroundoglycosylationsitesinmammalianproteins AT yurimukai structuralcharacteristicsaroundoglycosylationsitesinmammalianproteins |