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PDBsum entry 1ce7
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of mistletoe lectin i from viscum album.
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Authors
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R.Krauspenhaar,
S.Eschenburg,
M.Perbandt,
V.Kornilov,
N.Konareva,
I.Mikailova,
S.Stoeva,
R.Wacker,
T.Maier,
T.Singh,
A.Mikhailov,
W.Voelter,
C.Betzel.
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Ref.
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Biochem Biophys Res Commun, 1999,
257,
418-424.
[DOI no: ]
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PubMed id
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Abstract
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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 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.
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