1ouw: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ouw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Calystegia_sepium Calystegia sepium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OUW FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ouw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Calystegia_sepium Calystegia sepium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OUW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</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]] 1.37&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c3k|1c3k]], [[1c3m|1c3m]], [[1c3n|1c3n]]</div></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=1ouw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ouw OCA], [https://pdbe.org/1ouw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ouw RCSB], [https://www.ebi.ac.uk/pdbsum/1ouw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ouw 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=1ouw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ouw OCA], [https://pdbe.org/1ouw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ouw RCSB], [https://www.ebi.ac.uk/pdbsum/1ouw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ouw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LECC_CALSE LECC_CALSE] Mannose-binding lectin (PubMed:9111143, PubMed:18266762, PubMed:14561768, PubMed:26971576, PubMed:28973127). Preferentially binds mannose at concentrations ranging between 5 and 25 mM, but binds also glucose. Has a marked preference for methylated sugar derivatives, such as alpha-MeMan and alpha-MeGlc, at concentration down to 5 mM (PubMed:14561768). Binds to N-glycans, but not to glycolipid-type or other type of glycans (PubMed:28973127). Binds N-linked high-mannose-type glycans (PubMed:18266762, PubMed:28973127). Has a preference for smaller (Man(2)-Man(6)) high-mannose-type glycans to larger (Man(7)-Man(9)) ones. Recognizes both alpha1-6 extended and alpha1-3 extended monoantennary glycans. The addition of alpha1-2Man to the Man-alpha1-3Man-beta branch results in a significant loss of affinity, but beta1-2GlcNAc has some affinity. Has less affinity for biantennary glycans (PubMed:18266762). However, affinity is significant for the biantennary complex-type N-glycans with bisecting GlcNAc (PubMed:18266762, PubMed:26971576, PubMed:28973127). No affinity is observed for tri- and tetra-antennary glycans (PubMed:18266762). Binds bisected glycans of the mouse brain. Selectively binds to bisecting N-glycans which are in back-fold conformation, and does not favor a glycan with an extend conformation (PubMed:26971576). Has hemagglutinating activity against rabbit erythrocytes at 0.3 ug/ml and against trypsin-treated human erythrocytes at 5 ug/ml. Has mitogenic activity in murine cells (PubMed:9111143).<ref>PMID:14561768</ref> <ref>PMID:18266762</ref> <ref>PMID:26971576</ref> <ref>PMID:28973127</ref> <ref>PMID:9111143</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1ouw ConSurf].
</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=1ouw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant lectins display small variations within a single family. The crystal structure of the mannose-binding jacalin-related lectin from Calystegia sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa exhibits the same beta-prism fold as identified previously for other members of the family, but the shape and the hydrophobic character of its carbohydrate-binding site is unlike that of other members, consistent with surface plasmon resonance analysis showing a preference for methylated sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to those described earlier for Heltuba and jacalin but mimics the canonical 12-stranded beta-sandwich dimer found in legume lectins. The present structure exemplifies the adaptability of the beta-prism building block in the evolution of plant lectins and highlights the biological role of these quaternary structures for carbohydrate recognition.
The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold.,Bourne Y, Roig-Zamboni V, Barre A, Peumans WJ, Astoul CH, Van Damme EJ, Rouge P J Biol Chem. 2004 Jan 2;279(1):527-33. Epub 2003 Oct 15. PMID:14561768<ref>PMID:14561768</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ouw" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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[[Category: Calystegia sepium]]
[[Category: Calystegia sepium]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Astoul, C H]]
[[Category: Astoul CH]]
[[Category: Barre, A]]
[[Category: Barre A]]
[[Category: Bourne, Y]]
[[Category: Bourne Y]]
[[Category: Damme, E J.M van]]
[[Category: Peumans WJ]]
[[Category: Peumans, W J]]
[[Category: Roig-Zamboni V]]
[[Category: Roig-Zamboni, V]]
[[Category: Rouge P]]
[[Category: Rouge, P]]
[[Category: Van Damme EJM]]
[[Category: Agglutinin]]
[[Category: Beta-prism fold]]
[[Category: Jacalin-related]]
[[Category: Lectin]]
[[Category: Mannose-binding]]
[[Category: Sugar binding protein]]
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