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| {{STRUCTURE_1ce7| PDB=1ce7 | SCENE= }} | | {{STRUCTURE_1ce7| PDB=1ce7 | SCENE= }} |
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| '''MISTLETOE LECTIN I FROM VISCUM ALBUM'''
| | ===MISTLETOE LECTIN I FROM VISCUM ALBUM=== |
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| ==Overview==
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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. | | The line below this paragraph, {{ABSTRACT_PUBMED_10198229}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10198229 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10198229}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Wacker, R.]] | | [[Category: Wacker, R.]] |
| [[Category: Ribosome-inactivating protein type ii]] | | [[Category: Ribosome-inactivating protein type ii]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:37:51 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:37:25 2008'' |