1y2v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1y2v.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1y2v.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1y2v| PDB=1y2v | SCENE= }}
{{STRUCTURE_1y2v| PDB=1y2v | SCENE= }}
-
'''Crystal structure of the common edible mushroom (Agaricus bisporus) lectin in complex with T-antigen'''
+
===Crystal structure of the common edible mushroom (Agaricus bisporus) lectin in complex with T-antigen===
-
==Overview==
+
<!--
-
The lectin from the common mushroom Agaricus bisporus, the most popular edible species in Western countries, has potent antiproliferative effects on human epithelial cancer cells, without any apparent cytotoxicity. This property confers to it an important therapeutic potential as an antineoplastic agent. The three-dimensional structure of the lectin was determined by x-ray diffraction. The protein is a tetramer with 222 symmetry, and each monomer presents a novel fold with two beta sheets connected by a helix-loop-helix motif. Selectivity was studied by examining the binding of four monosaccharides and seven disaccharides in two different crystal forms. The T-antigen disaccharide, Galbeta1-3GalNAc, mediator of the antiproliferative effects of the protein, binds at a shallow depression on the surface of the molecule. The binding of N-acetylgalactosamine overlaps with that moiety of the T antigen, but surprisingly, N-acetylglucosamine, which differs from N-acetylgalactosamine only in the configuration of epimeric hydroxyl 4, binds at a totally different site on the opposite side of the helix-loop-helix motif. The lectin thus has two distinct binding sites per monomer that recognize the different configuration of a single epimeric hydroxyl. The structure of the protein and its two carbohydrate-binding sites are described in detail in this study.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15596442}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15596442 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15596442}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
The antineoplastic lectin of the common edible mushroom (Agaricus bisporus) has two binding sites, each specific for a different configuration at a single epimeric hydroxyl., Carrizo ME, Capaldi S, Perduca M, Irazoqui FJ, Nores GA, Monaco HL, J Biol Chem. 2005 Mar 18;280(11):10614-23. Epub 2004 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15596442 15596442]
The antineoplastic lectin of the common edible mushroom (Agaricus bisporus) has two binding sites, each specific for a different configuration at a single epimeric hydroxyl., Carrizo ME, Capaldi S, Perduca M, Irazoqui FJ, Nores GA, Monaco HL, J Biol Chem. 2005 Mar 18;280(11):10614-23. Epub 2004 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15596442 15596442]
 +
 +
Crystallization and preliminary X-ray study of the common edible mushroom (Agaricus bisporus) lectin., Carrizo ME, Irazoqui FJ, Lardone RD, Nores GA, Curtino JA, Capaldi S, Perduca M, Monaco HL, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):718-20. Epub 2004, Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15039564 15039564]
[[Category: Agaricus bisporus]]
[[Category: Agaricus bisporus]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 33: Line 39:
[[Category: Mushroom]]
[[Category: Mushroom]]
[[Category: T-antigen]]
[[Category: T-antigen]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:49:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:32:55 2008''

Revision as of 11:32, 28 July 2008

Image:1y2v.png

Template:STRUCTURE 1y2v

Crystal structure of the common edible mushroom (Agaricus bisporus) lectin in complex with T-antigen

Template:ABSTRACT PUBMED 15596442

About this Structure

1Y2V is a Single protein structure of sequence from Agaricus bisporus. Full crystallographic information is available from OCA.

Reference

The antineoplastic lectin of the common edible mushroom (Agaricus bisporus) has two binding sites, each specific for a different configuration at a single epimeric hydroxyl., Carrizo ME, Capaldi S, Perduca M, Irazoqui FJ, Nores GA, Monaco HL, J Biol Chem. 2005 Mar 18;280(11):10614-23. Epub 2004 Dec 13. PMID:15596442

Crystallization and preliminary X-ray study of the common edible mushroom (Agaricus bisporus) lectin., Carrizo ME, Irazoqui FJ, Lardone RD, Nores GA, Curtino JA, Capaldi S, Perduca M, Monaco HL, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):718-20. Epub 2004, Mar 23. PMID:15039564

Page seeded by OCA on Mon Jul 28 14:32:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y2v"
Personal tools