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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[1uh0]] 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=1UH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UH0 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1uh0]] 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=1UH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UH0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MGC:ALPHA-METHYL-N-ACETYL-D-GALACTOSAMINE'>MGC</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]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m26|1m26]], [[1jac|1jac]], [[1ugw|1ugw]], [[1ugx|1ugx]], [[1ugy|1ugy]], [[1uh1|1uh1]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MGC:ALPHA-METHYL-N-ACETYL-D-GALACTOSAMINE'>MGC</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=1uh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uh0 OCA], [https://pdbe.org/1uh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uh0 RCSB], [https://www.ebi.ac.uk/pdbsum/1uh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uh0 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=1uh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uh0 OCA], [https://pdbe.org/1uh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uh0 RCSB], [https://www.ebi.ac.uk/pdbsum/1uh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uh0 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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| | [[Category: Artocarpus integer]] | | [[Category: Artocarpus integer]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jeyaprakash, A A]] | + | [[Category: Jeyaprakash AA]] |
| - | [[Category: Katiyar, S]] | + | [[Category: Katiyar S]] |
| - | [[Category: Sekar, K]] | + | [[Category: Sekar K]] |
| - | [[Category: Surolia, A]] | + | [[Category: Surolia A]] |
| - | [[Category: Swaminathan, C P]] | + | [[Category: Swaminathan CP]] |
| - | [[Category: Vijayan, M]] | + | [[Category: Vijayan M]] |
| - | [[Category: All beta sheet protein]]
| + | |
| - | [[Category: Beta-prism i fold]]
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| - | [[Category: Gal specific]]
| + | |
| - | [[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 structures of the complexes of tetrameric jacalin with Gal, Me-alpha-GalNAc, Me-alpha-T-antigen, GalNAcbeta1-3Gal-alpha-O-Me and Galalpha1-6Glc (mellibiose) show that the sugar-binding site of jacalin has three components: the primary site, secondary site A, and secondary site B. In these structures and in the two structures reported earlier, Gal or GalNAc occupy the primary site with the anomeric carbon pointing towards secondary site A. The alpha-substituents, when present, interact, primarily hydrophobically, with secondary site A which has variable geometry. O-H..., centered pi and C-H...pi hydrogen bonds involving this site also exist. On the other hand, beta-substitution leads to severe steric clashes. Therefore, in complexes involving beta-linked disaccharides, the reducing sugar binds at the primary site with the non-reducing end located at secondary site B. The interactions at secondary site B are primarily through water bridges. Thus, the nature of the linkage determines the mode of the association of the sugar with jacalin. The interactions observed in the crystal structures and modeling based on them provide a satisfactory qualitative explanation of the available thermodynamic data on jacalin-carbohydrate interactions. They also lead to fresh insights into the nature of the binding of glycoproteins by jacalin.
Structural basis of the carbohydrate specificities of jacalin: an X-ray and modeling study.,Jeyaprakash AA, Katiyar S, Swaminathan CP, Sekar K, Surolia A, Vijayan M J Mol Biol. 2003 Sep 5;332(1):217-28. PMID:12946359[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jeyaprakash AA, Katiyar S, Swaminathan CP, Sekar K, Surolia A, Vijayan M. Structural basis of the carbohydrate specificities of jacalin: an X-ray and modeling study. J Mol Biol. 2003 Sep 5;332(1):217-28. PMID:12946359
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