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| | <StructureSection load='1uha' size='340' side='right'caption='[[1uha]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='1uha' size='340' side='right'caption='[[1uha]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uha]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UHA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uha]] is a 1 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=1UHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UHA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uha OCA], [http://pdbe.org/1uha PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uha RCSB], [http://www.ebi.ac.uk/pdbsum/1uha PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uha ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1uha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uha OCA], [https://pdbe.org/1uha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uha RCSB], [https://www.ebi.ac.uk/pdbsum/1uha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uha ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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/uh/1uha_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uh/1uha_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: Hamasu, M]] | + | [[Category: Hamasu M]] |
| - | [[Category: Hata, Y]] | + | [[Category: Hata Y]] |
| - | [[Category: Hayashida, M]] | + | [[Category: Hayashida M]] |
| - | [[Category: Ishiguro, M]] | + | [[Category: Ishiguro M]] |
| - | [[Category: Chitin-binding domain]]
| + | |
| - | [[Category: Lectin]]
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| - | [[Category: Sugar binding protein]]
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| 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
Pokeweed lectin (PL), a lectin specific for N-acetylglucosamine-containing saccharides, stimulates peripheral lymphocytes to undergo mitosis by binding to their cell surfaces. Four types of lectins have been isolated from the roots of pokeweed (Phytolacca americana) and shown to contain homologous domains but to have different molecular sizes and biological properties. PL-D, the smallest lectin in the group, has two isolectins, PL-D1 and PL-D2. PL-D1 consists of 84 amino-acid residues, while PL-D2 is identical to PL-D1 in sequence except for the lack of two C-terminal residues, Leu83 and Thr84. The crystal structures of PL-D1 and PL-D2 were solved by the molecular-replacement method and refined to 1.65 and 1.5 A resolution with R factors of 17.2 and 17.6%, respectively. The PL-Ds are composed of two repetitive chitin-binding domains, each of which has four S-S bridges and one putative carbohydrate-binding site. The two carbohydrate-binding sites in PL-D are located on one side of the molecule. The relative orientation of the two domains in PL-D1 differs from that in PL-D2. Two C-terminal residues of PL-D1 are invisible in the present crystal structure, indicating the flexibility of the region. PL-D2 has a Ca2+ ion bound to the C-terminus on the molecular surface. A wide distribution of acidic residues is characteristically observed on one side of the C-terminal region of PL-D.
Structures of two lectins from the roots of pokeweed (Phytolacca americana).,Fujii T, Hayashida M, Hamasu M, Ishiguro M, Hata Y Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):665-73. Epub 2004, Mar 23. PMID:15039554[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
- ↑ Fujii T, Hayashida M, Hamasu M, Ishiguro M, Hata Y. Structures of two lectins from the roots of pokeweed (Phytolacca americana). Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):665-73. Epub 2004, Mar 23. PMID:15039554 doi:10.1107/S090744490400232X
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