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[[Image:1ulk.jpg|left|200px]]


{{Structure
==Crystal Structure of Pokeweed Lectin-C==
|PDB= 1ulk |SIZE=350|CAPTION= <scene name='initialview01'>1ulk</scene>, resolution 1.80&Aring;
<StructureSection load='1ulk' size='340' side='right'caption='[[1ulk]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1ulk]] 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=1ULK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULK FirstGlance]. <br>
|ACTIVITY=  
</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>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ulk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulk OCA], [https://pdbe.org/1ulk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ulk RCSB], [https://www.ebi.ac.uk/pdbsum/1ulk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ulk ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[1ulm|1ULM]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ulk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulk OCA], [http://www.ebi.ac.uk/pdbsum/1ulk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ulk RCSB]</span>
[https://www.uniprot.org/uniprot/LECC_PHYAM LECC_PHYAM] N-acetyl-D-glucosamine binding lectin. Almost no hemagglutinating activity towards human erythrocytes. Low mitogenic activity towards human peripheral blood lymphocytes.<ref>PMID:7772833</ref> <ref>PMID:7670205</ref>
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''Crystal Structure of Pokeweed Lectin-C'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ul/1ulk_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ulk ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.
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.


==About this Structure==
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<ref>PMID:14623194</ref>
1ULK is a [[Single protein]] structure of 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=1ULK OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://www.ncbi.nlm.nih.gov/pubmed/14623194 14623194]
</div>
<div class="pdbe-citations 1ulk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Phytolacca americana]]
[[Category: Phytolacca americana]]
[[Category: Single protein]]
[[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 protein]]
[[Category: hevein domain]]
[[Category: lectin]]
[[Category: pl-c]]
 
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