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1y2t

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Revision as of 12:40, 11 September 2015

Crystal structure of the common edible mushroom (Agaricus bisporus) lectin

Structural highlights

1y2t is a 2 chain structure with sequence from Agaricus bisporus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1y2u, 1y2v, 1y2w, 1y2x
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ABL_AGABI] Lectin that recognizes O-linked galactose-beta-1,3-N-acetylgalactosamine, a disaccharide (Thomsen-Friedenreich antigen or T-disaccharide), present on cell surface glycoproteins. Can also bind galactose-beta-1,3-N-acetylglucosamine. Does not bind monosaccharides. Can be internalized by clathrin-coated vesicles after binding to surface glycoproteins. After internalization it inhibits nuclear import of nuclear localization signal dependent proteins. Inhibits proliferation of malignant cells without cytotoxicity for normal cells.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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 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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Presant CA, Kornfeld S. Characterization of the cell surface receptor for the Agaricus bisporus hemagglutinin. J Biol Chem. 1972 Nov 10;247(21):6937-45. PMID:4343164
↑ Yu L, Fernig DG, Smith JA, Milton JD, Rhodes JM. Reversible inhibition of proliferation of epithelial cell lines by Agaricus bisporus (edible mushroom) lectin. Cancer Res. 1993 Oct 1;53(19):4627-32. PMID:8402638
↑ Yu LG, Fernig DG, White MR, Spiller DG, Appleton P, Evans RC, Grierson I, Smith JA, Davies H, Gerasimenko OV, Petersen OH, Milton JD, Rhodes JM. Edible mushroom (Agaricus bisporus) lectin, which reversibly inhibits epithelial cell proliferation, blocks nuclear localization sequence-dependent nuclear protein import. J Biol Chem. 1999 Feb 19;274(8):4890-9. PMID:9988731
↑ Carrizo ME, Capaldi S, Perduca M, Irazoqui FJ, Nores GA, Monaco HL. 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. J Biol Chem. 2005 Mar 18;280(11):10614-23. Epub 2004 Dec 13. PMID:15596442 doi:10.1074/jbc.M411989200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y2t"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1y2t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agaricus_bisporus Agaricus bisporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y2T FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y2u|1y2u]], [[1y2v|1y2v]], [[1y2w|1y2w]], [[1y2x|1y2x]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1y2t RCSB], [http://www.ebi.ac.uk/pdbsum/1y2t PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2t OCA], [http://pdbe.org/1y2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y2t RCSB], [http://www.ebi.ac.uk/pdbsum/1y2t PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1y2t" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1y2t

From Proteopedia

Revision as of 12:40, 11 September 2015

Crystal structure of the common edible mushroom (Agaricus bisporus) lectin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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