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[[Image:1m26.gif|left|200px]]


{{Structure
==Crystal structure of jacalin-T-antigen complex==
|PDB= 1m26 |SIZE=350|CAPTION= <scene name='initialview01'>1m26</scene>, resolution 1.62&Aring;
<StructureSection load='1m26' size='340' side='right'caption='[[1m26]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1m26]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Artocarpus_integer Artocarpus integer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M26 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</td></tr>
|GENE=  
<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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900084:Thomsen-Friedenreich+antigen'>PRD_900084</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=1m26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m26 OCA], [https://pdbe.org/1m26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m26 RCSB], [https://www.ebi.ac.uk/pdbsum/1m26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m26 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LECA_ARTIN LECA_ARTIN] D-galactose-specific lectin, binds the T-antigen structure Gal-beta1,3-GalNAc (Thomsen-Friedenreich-antigen-specific lectin). Potent and selective stimulant of distinct T- and B-cell functions. Shows a unique ability to specifically recognize IgA-1 from human serum.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m2/1m26_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m26 ConSurf].
<div style="clear:both"></div>


'''Crystal structure of jacalin-T-antigen complex'''
==See Also==
 
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Thomsen-Friedenreich antigen (Galbeta1-3GalNAc), generally known as T-antigen, is expressed in more than 85% of human carcinomas. Therefore, proteins which specifically bind T-antigen have potential diagnostic value. Jacalin, a lectin from jack fruit (Artocarpus integrifolia) seeds, is a tetramer of molecular mass 66kDa. It is one of the very few proteins which are known to bind T-antigen. The crystal structure of the jacalin-T-antigen complex has been determined at 1.62A resolution. The interactions of the disaccharide at the binding site are predominantly through the GalNAc moiety, with Gal interacting only through water molecules. They include a hydrogen bond between the anomeric oxygen of GalNAc and the pi electrons of an aromatic side-chain. Several intermolecular interactions involving the bound carbohydrate contribute to the stability of the crystal structure. The present structure, along with that of the Me-alpha-Gal complex, provides a reasonable qualitative explanation for the known affinities of jacalin to different carbohydrate ligands and a plausible model of the binding of the lectin to T-antigen O-linked to seryl or threonyl residues. Including the present one, the structures of five lectin-T-antigen complexes are available. GalNAc occupies the primary binding site in three of them, while Gal occupies the site in two. The choice appears to be related to the ability of the lectin to bind sialylated sugars. In either case, most of the lectin-disaccharide interactions are at the primary binding site. The conformation of T-antigen in the five complexes is nearly the same.
[[Category: Artocarpus integer]]
 
[[Category: Large Structures]]
==About this Structure==
[[Category: Banumathi S]]
1M26 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Artocarpus_integrifolia Artocarpus integrifolia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M26 OCA].
[[Category: Betzel C]]
 
[[Category: Jeyaprakash AA]]
==Reference==
[[Category: Rani PG]]
Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes., Jeyaprakash AA, Geetha Rani P, Banuprakash Reddy G, Banumathi S, Betzel C, Sekar K, Surolia A, Vijayan M, J Mol Biol. 2002 Aug 23;321(4):637-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12206779 12206779]
[[Category: Reddy GB]]
[[Category: Artocarpus integrifolia]]
[[Category: Surolia A]]
[[Category: Protein complex]]
[[Category: Vijayan M]]
[[Category: Banumathi, S.]]
[[Category: Betzel, C.]]
[[Category: Jeyaprakash, A A.]]
[[Category: Rani, P G.]]
[[Category: Reddy, G B.]]
[[Category: Surolia, A.]]
[[Category: Vijayan, M.]]
[[Category: all beta sheet protein]]
[[Category: beta prism i fold]]
 
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Retrieved from "https://proteopedia.org/1m26"