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| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1ulm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULM FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1ulm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULM FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 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;'>[[1ulk|1ulk]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</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=1ulm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulm OCA], [https://pdbe.org/1ulm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ulm RCSB], [https://www.ebi.ac.uk/pdbsum/1ulm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ulm 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=1ulm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulm OCA], [https://pdbe.org/1ulm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ulm RCSB], [https://www.ebi.ac.uk/pdbsum/1ulm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ulm ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/LED2_PHYAM LED2_PHYAM]] N-acetyl-D-glucosamine binding lectin. Shows no hemagglutinating activity towards rabbit erythrocytes and weak activity towards trypsin-treated erythrocytes. Has mitogenic activity towards human peripheral blood lymphocytes (HPBL).<ref>PMID:8987560</ref> <ref>PMID:15277769</ref> <ref>PMID:14623194</ref>
| + | [https://www.uniprot.org/uniprot/LED2_PHYAM LED2_PHYAM] N-acetyl-D-glucosamine binding lectin. Shows no hemagglutinating activity towards rabbit erythrocytes and weak activity towards trypsin-treated erythrocytes. Has mitogenic activity towards human peripheral blood lymphocytes (HPBL).<ref>PMID:8987560</ref> <ref>PMID:15277769</ref> <ref>PMID:14623194</ref> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| <jmolCheckbox> | | <jmolCheckbox> |
| <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ul/1ulm_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ul/1ulm_consurf.spt"</scriptWhenChecked> |
- | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| </jmolCheckbox> | | </jmolCheckbox> |
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Phytolacca americana]] | | [[Category: Phytolacca americana]] |
- | [[Category: Fujii, T]] | + | [[Category: Fujii T]] |
- | [[Category: Hata, Y]] | + | [[Category: Hata Y]] |
- | [[Category: Hayashida, M]] | + | [[Category: Hayashida M]] |
- | [[Category: Ishiguro, M]] | + | [[Category: Ishiguro M]] |
- | [[Category: Chitin-binding]]
| + | |
- | [[Category: Hevein domain]]
| + | |
- | [[Category: Lectin]]
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- | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
LED2_PHYAM N-acetyl-D-glucosamine binding lectin. Shows no hemagglutinating activity towards rabbit erythrocytes and weak activity towards trypsin-treated erythrocytes. Has mitogenic activity towards human peripheral blood lymphocytes (HPBL).[1] [2] [3]
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 roots of pokeweed (Phytolacca americana) are known to contain the lectins designated PL-A, PL-B, PL-C, PL-D1, and PL-D2. Of these lectins, the crystal structures of two PLs, the ligand-free PL-C and the complex of PL-D2 with tri-N-acetylchitotriose, have been determined at 1.8A resolution. The polypeptide chains of PL-C and PL-D2 form three and two repetitive chitin-binding domains, respectively. In the crystal structure of the PL-D2 complex, one trisaccharide molecule is shared mainly between two neighboring molecules related to each other by a crystallographic 2(1)-screw axis, and infinite helical chains of complexed molecules are generated by the sharing of ligand molecules. The crystal structure of PL-C reveals that the molecule is a dimer of two identical subunits, whose polypeptide chains are located in a head-to-tail fashion by a molecular 2-fold axis. Three putative carbohydrate-binding sites in each subunit are located in the dimer interface. The dimerization of PL-C is performed through the hydrophobic interactions between the carbohydrate-binding sites of the opposite domains in the dimer, leading to a distinct dimerization mode from that of wheat-germ agglutinin. Three aromatic residues in each carbohydrate-binding site of PL-C are involved in the dimerization. These residues correspond to the residues that interact mainly with the trisaccharide in the PL-D2 complex and appear to mimic the saccharide residues in the complex. Consequently, the present structure of the PL-C dimer has no room for accommodating carbohydrate. The quaternary structure of PL-C formed through these putative carbohydrate-binding residues may lead to the lack of hemagglutinating activity.
Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed.,Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y J Mol Biol. 2003 Nov 28;334(3):551-65. PMID:14623194[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yamaguchi K, Mori A, Funatsu G. Amino acid sequence and some properties of lectin-D from the roots of pokeweed (Phytolacca americana). Biosci Biotechnol Biochem. 1996 Aug;60(8):1380-2. PMID:8987560 doi:http://dx.doi.org/10.1271/bbb.60.1380
- ↑ Yamaguchi K, Uechi M, Katakura Y, Oda T, Ishiguro M. Mitogenic properties of pokeweed lectin-D isoforms on human peripheral blood lymphocytes: non-mitogen PL-D1 and mitogen PL-D2. Biosci Biotechnol Biochem. 2004 Jul;68(7):1591-3. PMID:15277769 doi:http://dx.doi.org/10.1271/bbb.68.1591
- ↑ Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y. Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed. J Mol Biol. 2003 Nov 28;334(3):551-65. PMID:14623194
- ↑ Hayashida M, Fujii T, Hamasu M, Ishiguro M, Hata Y. Similarity between protein-protein and protein-carbohydrate interactions, revealed by two crystal structures of lectins from the roots of pokeweed. J Mol Biol. 2003 Nov 28;334(3):551-65. PMID:14623194
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