3wsr
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3wsr is ON HOLD Authors: Nagae, M., Yamaguchi, Y. Description: Crystal structure of lectin-ligand complex) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of CLEC-2 in complex with O-glycosylated podoplanin== | |
| + | <StructureSection load='3wsr' size='340' side='right'caption='[[3wsr]], [[Resolution|resolution]] 1.91Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3wsr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WSR FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</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=3wsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wsr OCA], [https://pdbe.org/3wsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wsr RCSB], [https://www.ebi.ac.uk/pdbsum/3wsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wsr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CLC1B_HUMAN CLC1B_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Podoplanin is a transmembrane O-glycoprotein that binds to C-type lectin-like receptor 2 (CLEC-2). The O-glycan-dependent interaction seems to play crucial roles in various biological processes, such as platelet aggregation. Rhodocytin, a snake venom, also binds to CLEC-2 and aggregates platelets in a glycan-independent manner. To elucidate the structural basis of the glycan-dependent and independent interactions, we performed comparative crystallographic studies of podoplanin and rhodocytin in complex with CLEC-2. Both podoplanin and rhodocytin bind to the noncanonical "side" face of CLEC-2. There is a common interaction mode between consecutive acidic residues on the ligands and the same arginine residues on CLEC-2. Other interactions are ligand-specific. Carboxyl groups from the sialic acid residue on podoplanin and from the C terminus of the rhodocytin alpha subunit interact differently at this "second" binding site on CLEC-2. The unique and versatile binding modes open a way to understand the functional consequences of CLEC-2-ligand interactions. | ||
| - | + | A Platform of C-type Lectin-like Receptor CLEC-2 for Binding O-Glycosylated Podoplanin and Nonglycosylated Rhodocytin.,Nagae M, Morita-Matsumoto K, Kato M, Kaneko MK, Kato Y, Yamaguchi Y Structure. 2014 Dec 2;22(12):1711-21. doi: 10.1016/j.str.2014.09.009. Epub 2014, Nov 6. PMID:25458834<ref>PMID:25458834</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3wsr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kato M]] | ||
| + | [[Category: Kato Y]] | ||
| + | [[Category: Kato-Kaneko M]] | ||
| + | [[Category: Morita-Matsumoto K]] | ||
| + | [[Category: Nagae M]] | ||
| + | [[Category: Yamaguchi Y]] | ||
Current revision
Crystal structure of CLEC-2 in complex with O-glycosylated podoplanin
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