Isomerization of Aspartic Acid in Protein.
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- NOGUCHI Shuji
- Graduate School of Pharmaceutical Sciences, University of Tokyo
Bibliographic Information
- Other Title
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- 蛋白質におけるアスパラギン酸の異性化
- タンパクシツ ニ オケル アスパラギンサン ノ イセイカ
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Abstract
Aspartic acid in protein isomerizes autocatalytically to isoaspartate via succinimide intermediate in vitro and in vivo. We have determined the crystal structures of Ustilago sphaerogena ribonuclease U2 with an isoaspartate residue and hen egg-white lysozymes with a succinimide intermediate and with an isoaspartate residue at 1.8 Å resolution. These crystal structures reveal that the isomerizations of aspartic acids induce structural changes on proteins, which result in modifying the function and physical properties of the proteins.
Journal
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- Nihon Kessho Gakkaishi
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Nihon Kessho Gakkaishi 40 (4), 272-278, 1998
The Crystallographic Society of Japan
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Details 詳細情報について
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- CRID
- 1390001204086993408
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- NII Article ID
- 10002590884
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- NII Book ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL BIB ID
- 4553534
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed
