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| [[Image:1hwp.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1hwp| PDB=1hwp | SCENE= }} | | {{STRUCTURE_1hwp| PDB=1hwp | SCENE= }} |
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| '''EBULIN COMPLEXED WITH PTEROIC ACID, TRIGONAL CRYSTAL FORM'''
| | ===EBULIN COMPLEXED WITH PTEROIC ACID, TRIGONAL CRYSTAL FORM=== |
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| ==Overview==
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| Ebulin l is a type-II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus L. As with other type-II RIP, ebulin is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. A normal level of ribosome-inactivating N-glycosidase activity, characteristic of the A chain of type-II RIP, has been demonstrated for ebulin l. However, ebulin is considered a nontoxic type-II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type-II RIP like ricin. The molecular cloning, amino acid sequence, and the crystal structure of ebulin l are presented and compared with ricin. Ebulin l is shown to bind an A-chain substrate analogue, pteroic acid, in the same manner as ricin. The galactoside-binding ability of ebulin l is demonstrated crystallographically with a complex of the B chain with galactose and with lactose. The negligible cytotoxicity of ebulin l is apparently due to a reduced affinity for galactosides. An altered mode of galactoside binding in the 2gamma subdomain of the lectin B chain primarily causes the reduced affinity.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11288182}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11288182 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11288182}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Ribosome-inactivating protein]] | | [[Category: Ribosome-inactivating protein]] |
| [[Category: Ricin-like]] | | [[Category: Ricin-like]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:18:12 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:01:39 2008'' |
