1ce7
MISTLETOE LECTIN I FROM VISCUM ALBUM
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OverviewOverview
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.
About this StructureAbout this Structure
1CE7 is a Single protein structure of sequence from Viscum album with NAG as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of mistletoe lectin I from Viscum album., Krauspenhaar R, Eschenburg S, Perbandt M, Kornilov V, Konareva N, Mikailova I, Stoeva S, Wacker R, Maier T, Singh T, Mikhailov A, Voelter W, Betzel C, Biochem Biophys Res Commun. 1999 Apr 13;257(2):418-24. PMID:10198229
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