3wsr
From Proteopedia
(Difference between revisions)
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<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=3wsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wsr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wsr RCSB], [http://www.ebi.ac.uk/pdbsum/3wsr PDBsum]</span></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=3wsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wsr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wsr RCSB], [http://www.ebi.ac.uk/pdbsum/3wsr PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Kato, M | + | [[Category: Kato, M]] |
| - | [[Category: Kato, Y | + | [[Category: Kato, Y]] |
| - | [[Category: Kato-Kaneko, M | + | [[Category: Kato-Kaneko, M]] |
| - | [[Category: Morita-Matsumoto, K | + | [[Category: Morita-Matsumoto, K]] |
| - | [[Category: Nagae, M | + | [[Category: Nagae, M]] |
| - | [[Category: Yamaguchi, Y | + | [[Category: Yamaguchi, Y]] |
[[Category: C-type lectin fold]] | [[Category: C-type lectin fold]] | ||
[[Category: Cell surface receptor]] | [[Category: Cell surface receptor]] | ||
Revision as of 10:53, 24 December 2014
Crystal structure of CLEC-2 in complex with O-glycosylated podoplanin
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