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Crystal Structure of Mistletoe Lectin I fromViscum album
- Source :
- Biochemical and Biophysical Research Communications; April 1999, Vol. 257 Issue: 2 p418-424, 7p
- Publication Year :
- 1999
-
Abstract
- The crystal structure of the ribosome-inactivating protein (RIP) mistletoe lectin I (ML-I) fromViscum albumhas 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 Å 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 fromRicinus 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.
Details
- Language :
- English
- ISSN :
- 0006291X and 10902104
- Volume :
- 257
- Issue :
- 2
- Database :
- Supplemental Index
- Journal :
- Biochemical and Biophysical Research Communications
- Publication Type :
- Periodical
- Accession number :
- ejs668399
- Full Text :
- https://doi.org/10.1006/bbrc.1999.0470