Structural Biology of Post-translational Modifications of Proteins

• Kato Koichi

  Institute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences Graduate School of Pharmaceutical Sciences, Nagoya City University The Glycoscience Institute, Ochanomizu University GLYECE Co., Ltd.

Bibliographic Information

Other Title

• タンパク質の翻訳後修飾の構造生物学研究
• タンパクシツ ノ ホンヤク ゴ シュウショク ノ コウゾウ セイブツガク ケンキュウ

Abstract

  A majority of proteins encoded in genomes of limited size are post-translationally diversified by covalent modifications such as glycosylation and ubiquitination. Although recent advances in structural proteomics have enabled high-throughput structure determination of proteins, structural analyses of post-translationally modified proteins remain challenging because of the lack of appropriate determination methods. Therefore, we developed methodologies for characterizing the post-translational modifications of proteins from the structural viewpoint, focusing especially on glycosylation and ubiquitination. For instance, we established a systematic method for structural glycomics to address broader issues, including glycosylation profiling and 3D structure analyses of glycoproteins. Our stable-isotope-assisted NMR techniques in conjunction with X-ray crystallographic approach provide valuable information at the atomic level on conformations, dynamics, and interactions of glycoproteins such as antibody and proteins involved in the ubiquitin-proteasome system. These studies provide the structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans and mechanistic insights into ubiquitination reactions in glycoprotein-fate determination in cells. These approaches will allow new possibilities for structural studies on post-translationally modified proteins of clinical, pathological, and pharmaceutical interests.<br>

Journal

• YAKUGAKU ZASSHI

  YAKUGAKU ZASSHI 132 (5), 563-573, 2012-05-01

  The Pharmaceutical Society of Japan

Keywords

• glycosylation
• ubiquitination
• structural biology
• post-translational modification
• NMR spectroscopy
• X-ray crystallography

Details

• CRID: 1390001206126653440
• NII Article ID: 130001888672
• NII Book ID: AN00284903
• DOI: 10.1248/yakushi.132.563
• COI: 1:STN:280:DC%2BC38jgslKgtA%3D%3D
• ISSN: 13475231
• ISSN: 00316903
• NDL BIB ID: 023754048
• PubMed: 22687692
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I023754048
• Web Site: https://www.jstage.jst.go.jp/article/yakushi/132/5/132_5_563/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2012292047
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed