1n47
From Proteopedia
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[[Image:1n47.gif|left|200px]] | [[Image:1n47.gif|left|200px]] | ||
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'''Isolectin B4 from Vicia villosa in complex with the Tn antigen''' | '''Isolectin B4 from Vicia villosa in complex with the Tn antigen''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N47 OCA]. | |
==Reference== | ==Reference== | ||
The crystal structure of a plant lectin in complex with the Tn antigen., Babino A, Tello D, Rojas A, Bay S, Osinaga E, Alzari PM, FEBS Lett. 2003 Feb 11;536(1-3):106-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12586347 12586347] | The crystal structure of a plant lectin in complex with the Tn antigen., Babino A, Tello D, Rojas A, Bay S, Osinaga E, Alzari PM, FEBS Lett. 2003 Feb 11;536(1-3):106-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12586347 12586347] | ||
| - | [[Category: Protein complex]] | ||
| - | [[Category: Vicia villosa]] | ||
[[Category: Alzari, P M.]] | [[Category: Alzari, P M.]] | ||
[[Category: Babino, A.]] | [[Category: Babino, A.]] | ||
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[[Category: Rojas, A.]] | [[Category: Rojas, A.]] | ||
[[Category: Tello, D.]] | [[Category: Tello, D.]] | ||
| - | [[Category: | + | [[Category: Cancer antigen]] |
| - | [[Category: | + | [[Category: Carbohydrate recognition]] |
| - | [[Category: | + | [[Category: Glycoprotein tn-binding protein]] |
| - | [[Category: | + | [[Category: Vicia villosa lectin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:04:10 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:04, 2 May 2008
Isolectin B4 from Vicia villosa in complex with the Tn antigen
Overview
The structure of the tetrameric Vicia villosa isolectin B4 (VVLB4) in complex with a cancer antigen, the Tn glycopeptide (GalNAc-O-Ser), was determined at 2.7 A resolution. The N-acetylgalactoside moiety of the ligand binds to the primary combining site of VVLB4 in a similar way as observed for other Gal/GalNAc-specific plant lectins. The amino acid moiety of the Tn antigen is largely exposed to the solvent and makes few contacts with the protein. The structure of the complex provides a framework to understand the differences in the strength of VVLB4 binding to different sugars and emphasizes the role of a single protein residue, Tyr127, as a structural determinant of Tn-binding specificity.
About this Structure
Full crystallographic information is available from OCA.
Reference
The crystal structure of a plant lectin in complex with the Tn antigen., Babino A, Tello D, Rojas A, Bay S, Osinaga E, Alzari PM, FEBS Lett. 2003 Feb 11;536(1-3):106-10. PMID:12586347 Page seeded by OCA on Sat May 3 02:04:10 2008
