Crystal structure of mistletoe lectin I from Viscum album

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1999-04, Vol.257 (2), p.418
Main Authors: Krauspenhaar, R. (University Hospital, Hamburg, Germany.), Eschenburg, S, Perbandt, M, Kornilov, V, Konareva, N, Mikailova, I, Stoeva, S, Wacker, R, Maier, T, Singh, T
Format: Article
Language:English
Subjects:
Abrin - chemistry
Binding Sites
Conserved Sequence
Crystallization
Crystallography, X-Ray
Cysteine - chemistry
Cysteine - metabolism
Dimerization
Disulfides - chemistry
Disulfides - metabolism
Galactose - metabolism
Hydrogen Bonding
LECTINAS
LECTINE
LECTINS
Mistletoe - chemistry
Models, Molecular
PHARMACEUTICAL PRODUCTS
Plant Lectins
Plant Preparations
Plant Proteins
Plants, Medicinal
Protein Structure, Secondary
Ribosome Inactivating Proteins, Type 2
Ricin - chemistry
Static Electricity
Toxins, Biological - chemistry
Toxins, Biological - metabolism
Toxins, Biological - therapeutic use
VISCUM ALBUM
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1999.0470