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[[Image:1pxd.gif|left|200px]]
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{{STRUCTURE_1pxd|  PDB=1pxd  |  SCENE=  }}
'''Crystal structure of the complex of jacalin with meso-tetrasulphonatophenylporphyrin.'''


==Crystal structure of the complex of jacalin with meso-tetrasulphonatophenylporphyrin.==
<StructureSection load='1pxd' size='340' side='right'caption='[[1pxd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pxd]] is a 2 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=1PXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PXD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFP:5,10,15,20-TETRAKIS(4-SULPFONATOPHENYL)-21H,23H-PORPHINE'>SFP</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=1pxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pxd OCA], [https://pdbe.org/1pxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pxd RCSB], [https://www.ebi.ac.uk/pdbsum/1pxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pxd 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/px/1pxd_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=1pxd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the complex of meso-tetrasulfonatophenylporphyrin (H(2)TPPS) with jack fruit (Artocarpus integriflora) agglutinin (jacalin) has been determined at 1.8 A resolution. A porphyrin pair is sandwiched between two symmetry-related jacalin monomers in the crystal, leading to a cross-linking network of protein molecules. Apart from the stacking interactions, H(2)TPPS also forms hydrogen bonds, some involving water bridges, with jacalin at the carbohydrate-binding site. The residues that are involved in rendering galactopyranoside specificity to jacalin undergo conformational adjustments in order to accommodate the H(2)TPPS molecule. The water molecules at the carbohydrate-binding site of jacalin cement the jacalin-porphyrin interactions, optimizing their complementarity. Interactions of porphyrin with jacalin are relatively weak compared with those observed between galactopyranoside and jacalin, perhaps because the former largely involves water-mediated hydrogen bonds. While H(2)TPPS binds to jacalin at the carbohydrate-binding site as in the case of ConA, its mode of interaction with jacalin is very different. H(2)TPPS does not enter the carbohydrate-binding cavity of jacalin. Instead, it sits over the binding site. While the porphyrin binding is mediated by replicating the hydrogen-bonding network of mannopyranoside through the sulfonate atoms in the case of ConA, the plasticity associated with the carbohydrate-binding site accommodates the pluripotent porphyrin molecule in the case of jacalin through an entirely different set of interactions.


==Overview==
Porphyrin binding to jacalin is facilitated by the inherent plasticity of the carbohydrate-binding site: novel mode of lectin-ligand interaction.,Goel M, Anuradha P, Kaur KJ, Maiya BG, Swamy MJ, Salunke DM Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):281-8. Epub 2004, Jan 23. PMID:14747704<ref>PMID:14747704</ref>
The crystal structure of the complex of meso-tetrasulfonatophenylporphyrin (H(2)TPPS) with jack fruit (Artocarpus integriflora) agglutinin (jacalin) has been determined at 1.8 A resolution. A porphyrin pair is sandwiched between two symmetry-related jacalin monomers in the crystal, leading to a cross-linking network of protein molecules. Apart from the stacking interactions, H(2)TPPS also forms hydrogen bonds, some involving water bridges, with jacalin at the carbohydrate-binding site. The residues that are involved in rendering galactopyranoside specificity to jacalin undergo conformational adjustments in order to accommodate the H(2)TPPS molecule. The water molecules at the carbohydrate-binding site of jacalin cement the jacalin-porphyrin interactions, optimizing their complementarity. Interactions of porphyrin with jacalin are relatively weak compared with those observed between galactopyranoside and jacalin, perhaps because the former largely involves water-mediated hydrogen bonds. While H(2)TPPS binds to jacalin at the carbohydrate-binding site as in the case of ConA, its mode of interaction with jacalin is very different. H(2)TPPS does not enter the carbohydrate-binding cavity of jacalin. Instead, it sits over the binding site. While the porphyrin binding is mediated by replicating the hydrogen-bonding network of mannopyranoside through the sulfonate atoms in the case of ConA, the plasticity associated with the carbohydrate-binding site accommodates the pluripotent porphyrin molecule in the case of jacalin through an entirely different set of interactions.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1PXD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Artocarpus_integer Artocarpus integer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PXD OCA].
</div>
<div class="pdbe-citations 1pxd" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Porphyrin binding to jacalin is facilitated by the inherent plasticity of the carbohydrate-binding site: novel mode of lectin-ligand interaction., Goel M, Anuradha P, Kaur KJ, Maiya BG, Swamy MJ, Salunke DM, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):281-8. Epub 2004, Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14747704 14747704]
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Artocarpus integer]]
[[Category: Artocarpus integer]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Anuradha, P.]]
[[Category: Anuradha P]]
[[Category: Goel, M.]]
[[Category: Goel M]]
[[Category: Kaur, K J.]]
[[Category: Kaur KJ]]
[[Category: Maiya, B G.]]
[[Category: Maiya BG]]
[[Category: Salunke, D M.]]
[[Category: Salunke DM]]
[[Category: Swamy, M J.]]
[[Category: Swamy MJ]]
[[Category: Lectin]]
[[Category: Porphyrin]]
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