Crystal structure of mistletoe lectin I from Viscum album

Krauspenhaar, R. and Eschenburg, S. and Perbandt, M. and Kornilov, V. and Konareva, N. and Mikailova, I. and Stoeva, S. and Wacker, R. and Maier, T. and Singh, T. and Mikhailov, A. and Voelter, W. and Betzel, C.. (1999) Crystal structure of mistletoe lectin I from Viscum album. Biochemical and Biophysical Research Communications, 257 (2). pp. 418-424.

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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 Angstrom 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 hom 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. (C) 1999 Academic Press.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:26 Oct 2017 12:47
Deposited On:26 Oct 2017 12:47

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