1n47

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(New page: 200px<br /><applet load="1n47" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n47, resolution 2.70&Aring;" /> '''Isolectin B4 from Vi...)
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[[Image:1n47.gif|left|200px]]<br /><applet load="1n47" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n47.gif|left|200px]]<br /><applet load="1n47" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n47, resolution 2.70&Aring;" />
caption="1n47, resolution 2.70&Aring;" />
'''Isolectin B4 from Vicia villosa in complex with the Tn antigen'''<br />
'''Isolectin B4 from Vicia villosa in complex with the Tn antigen'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1N47 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vicia_villosa Vicia villosa] with CA, MN and TNR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N47 OCA].
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1N47 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vicia_villosa Vicia villosa] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=TNR:'>TNR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N47 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Vicia villosa]]
[[Category: Vicia villosa]]
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[[Category: Alzari, P.M.]]
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[[Category: Alzari, P M.]]
[[Category: Babino, A.]]
[[Category: Babino, A.]]
[[Category: Bay, S.]]
[[Category: Bay, S.]]
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[[Category: vicia villosa lectin]]
[[Category: vicia villosa lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:56:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:06 2008''

Revision as of 12:02, 21 February 2008


1n47, resolution 2.70Å

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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

1N47 is a Protein complex structure of sequences from Vicia villosa with , and as ligands. 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

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