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| | <StructureSection load='1pxd' size='340' side='right'caption='[[1pxd]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1pxd' size='340' side='right'caption='[[1pxd]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pxd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Artin Artin]. 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> | + | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jn2|1jn2]]</div></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> | | <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> | | </table> |
| | == Function == | | == 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. [[https://www.uniprot.org/uniprot/LECB3_ARTIN LECB3_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.
| + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Artin]] | + | [[Category: Artocarpus integer]] |
| | [[Category: Large Structures]] | | [[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]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
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
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 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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Goel M, Anuradha P, Kaur KJ, Maiya BG, Swamy MJ, Salunke DM. Porphyrin binding to jacalin is facilitated by the inherent plasticity of the carbohydrate-binding site: novel mode of lectin-ligand interaction. Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):281-8. Epub 2004, Jan 23. PMID:14747704 doi:10.1107/S0907444903026684
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