1CE7

MISTLETOE LECTIN I FROM VISCUM ALBUM

1CE7 の概要

• エントリーDOI: 10.2210/pdb1ce7/pdb
• 分子名称: PROTEIN (RIBOSOME-INACTIVATING PROTEIN TYPE II), 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: ribosome-inactivating protein type ii, ribosome
• 由来する生物種: Viscum album (European mistletoe); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53473.56

構造登録者

Krauspenhaar, R.,Eschenburg, S.,Perbandt, M.,Kornilov, V.,Konareva, N.,Mikailova, I.,Stoeva, S.,Wacker, R.,Maier, T.,Singh, T.P.,Mikhailov, A.,Voelter, W.,Betzel, C. (登録日: 1999-03-18, 公開日: 2000-03-20, 最終更新日: 2024-11-13)

主引用文献

Krauspenhaar, R.,Eschenburg, S.,Perbandt, M.,Kornilov, V.,Konareva, N.,Mikailova, I.,Stoeva, S.,Wacker, R.,Maier, T.,Singh, T.P.,Mikhailov, A.,Voelter, W.,Betzel, C.
Crystal structure of mistletoe lectin I from Viscum album.
Biochem.Biophys.Res.Commun., 257:418-424, 1999

PubMed Abstract: The crystal structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) from Viscum album has been solved by molecular replacement techniques. The structure has been refined to a crystallographic R-factor of 24.5% using X-ray diffraction data to 2.8 A resolution. The heterodimeric 63-kDa protein consists of a toxic A subunit which exhibits RNA-glycosidase activity and a galactose-specific lectin B subunit. The overall protein fold is similar to that of ricin from Ricinus communis; however, unlike ricin, ML-I is already medically applied as a component of a commercially available misteltoe extract with immunostimulating potency and for the treatment of human cancer. The three-dimensional structure reported here revealed structural details of this pharmaceutically important protein. The comparison to the structure of ricin gives more insights into the functional mechanism of this protein, provides structural details for further protein engineering studies, and may lead to the development of more effective therapeutic RIPs.

PubMed: 10198229
DOI: 10.1006/bbrc.1999.0470

実験手法

X-RAY DIFFRACTION (2.7 Å)