4d69: Difference between revisions

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==SOYBEAN AGGLUTININ FROM GLYCINE MAX IN COMPLEX WITH THE ANTIGEN Tn==
==SOYBEAN AGGLUTININ FROM GLYCINE MAX IN COMPLEX WITH THE ANTIGEN Tn==
<StructureSection load='4d69' size='340' side='right' caption='[[4d69]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='4d69' size='340' side='right'caption='[[4d69]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4d69]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] and [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D69 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D69 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4d69]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D69 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=4d69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d69 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d69 RCSB], [http://www.ebi.ac.uk/pdbsum/4d69 PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4d69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d69 OCA], [https://pdbe.org/4d69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d69 RCSB], [https://www.ebi.ac.uk/pdbsum/4d69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d69 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/LEC_SOYBN LEC_SOYBN]] Binds GalNAc and galactose.  
[https://www.uniprot.org/uniprot/LEC_SOYBN LEC_SOYBN] Binds GalNAc and galactose.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4d69" style="background-color:#fffaf0;"></div>
==See Also==
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Synthetic construct]]
[[Category: Asensio, J L]]
[[Category: Asensio JL]]
[[Category: Avenoza, A]]
[[Category: Avenoza A]]
[[Category: Busto, J H]]
[[Category: Busto JH]]
[[Category: Castro-Lopez, J]]
[[Category: Castro-Lopez J]]
[[Category: Coelho, H]]
[[Category: Coelho H]]
[[Category: Corzana, F]]
[[Category: Corzana F]]
[[Category: Hurtado-Guerrero, R]]
[[Category: Hurtado-Guerrero R]]
[[Category: Jimenez-Barbero, J]]
[[Category: Jimenez-Barbero J]]
[[Category: Madariaga, D]]
[[Category: Madariaga D]]
[[Category: Marcelo, F]]
[[Category: Marcelo F]]
[[Category: Martinez-Saez, N]]
[[Category: Martinez-Saez N]]
[[Category: Peregrina, J M]]
[[Category: Peregrina JM]]
[[Category: Somovilla, V J]]
[[Category: Somovilla VJ]]
[[Category: Valero-Gonzalez, J]]
[[Category: Valero-Gonzalez J]]
[[Category: Sugar-binding protein]]

Latest revision as of 15:21, 20 December 2023

SOYBEAN AGGLUTININ FROM GLYCINE MAX IN COMPLEX WITH THE ANTIGEN TnSOYBEAN AGGLUTININ FROM GLYCINE MAX IN COMPLEX WITH THE ANTIGEN Tn

Structural highlights

4d69 is a 24 chain structure with sequence from Glycine max and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEC_SOYBN Binds GalNAc and galactose.

Publication Abstract from PubMed

Tn antigen (alpha-O-GalNAc-Ser/Thr) is a convenient cancer biomarker that is recognized by antibodies and lectins. This work yields remarkable results for two plant lectins in terms of epitope recognition and reveals that these receptors show higher affinity for Tn antigen when it is incorporated in the Pro-Asp-Thr-Arg (PDTR) peptide region of mucin MUC1. In contrast, a significant affinity loss is observed when Tn antigen is located in the Ala-His-Gly-Val-Thr-Ser-Ala (AHGVTSA) or Ala-Pro-Gly-Ser-Thr-Ala-Pro (APGSTAP) fragments. Our data indicate that the charged residues, Arg and Asp, present in the PDTR sequence establish noteworthy fundamental interactions with the lectin surface as well as fix the conformation of the peptide backbone, favoring the presentation of the sugar moiety toward the lectin. These results may help to better understand glycopeptide-lectin interactions and may contribute to engineer new binding sites, allowing novel glycosensors for Tn antigen detection to be designed.

Detection of Tumor-Associated Glycopeptides by Lectins: The Peptide Context Modulates Carbohydrate Recognition.,Madariaga D, Martinez-Saez N, Somovilla VJ, Coelho H, Valero-Gonzalez J, Castro-Lopez J, Asensio JL, Jimenez-Barbero J, Busto JH, Avenoza A, Marcelo F, Hurtado-Guerrero R, Corzana F, Peregrina JM ACS Chem Biol. 2014 Dec 10. PMID:25457745[1]

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

See Also

References

  1. Madariaga D, Martinez-Saez N, Somovilla VJ, Coelho H, Valero-Gonzalez J, Castro-Lopez J, Asensio JL, Jimenez-Barbero J, Busto JH, Avenoza A, Marcelo F, Hurtado-Guerrero R, Corzana F, Peregrina JM. Detection of Tumor-Associated Glycopeptides by Lectins: The Peptide Context Modulates Carbohydrate Recognition. ACS Chem Biol. 2014 Dec 10. PMID:25457745 doi:http://dx.doi.org/10.1021/cb500855x

4d69, resolution 2.70Å

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