2015年
Structural characteristics around O-glycosylation sites in mammalian proteins
Journal of Biomechanical Science and Engineering
- ,
- 巻
- 10
- 号
- 1
- 開始ページ
- 1
- 終了ページ
- 6
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1299/jbse.14-00249
- 出版者・発行元
- Japan Society of Mechanical Engineers
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.
- ID情報
-
- DOI : 10.1299/jbse.14-00249
- ISSN : 1880-9863
- SCOPUS ID : 84929455536