1ce7
From Proteopedia
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'''MISTLETOE LECTIN I FROM VISCUM ALBUM''' | '''MISTLETOE LECTIN I FROM VISCUM ALBUM''' | ||
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[[Category: Voelter, W.]] | [[Category: Voelter, W.]] | ||
[[Category: Wacker, R.]] | [[Category: Wacker, R.]] | ||
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Revision as of 09:37, 2 May 2008
MISTLETOE LECTIN I FROM VISCUM ALBUM
Overview
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 Structure
1CE7 is a Single protein structure of sequence from Viscum album. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 12:37:51 2008
