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| | ==Crystal structure of CLEC-2 in complex with rhodocytin== | | ==Crystal structure of CLEC-2 in complex with rhodocytin== |
| - | <StructureSection load='3wwk' size='340' side='right' caption='[[3wwk]], [[Resolution|resolution]] 2.98Å' scene=''> | + | <StructureSection load='3wwk' size='340' side='right'caption='[[3wwk]], [[Resolution|resolution]] 2.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wwk]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma rhodostoma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WWK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WWK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wwk]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma rhodostoma] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WWK FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wsr|3wsr]]</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]] 2.98Å</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=3wwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwk OCA], [http://pdbe.org/3wwk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wwk RCSB], [http://www.ebi.ac.uk/pdbsum/3wwk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwk 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=3wwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wwk OCA], [https://pdbe.org/3wwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wwk RCSB], [https://www.ebi.ac.uk/pdbsum/3wwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wwk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CLC1B_HUMAN CLC1B_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Calloselasma rhodostoma]] | | [[Category: Calloselasma rhodostoma]] |
| - | [[Category: Kato, M]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kato, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Kato-Kaneko, M]] | + | [[Category: Kato M]] |
| - | [[Category: Morita-Matsumoto, K]] | + | [[Category: Kato Y]] |
| - | [[Category: Nagae, M]] | + | [[Category: Kato-Kaneko M]] |
| - | [[Category: Yamaguchi, Y]] | + | [[Category: Morita-Matsumoto K]] |
| - | [[Category: C-type lectin fold]]
| + | [[Category: Nagae M]] |
| - | [[Category: Carbohydrate binding]] | + | [[Category: Yamaguchi Y]] |
| - | [[Category: Podoplanin]] | + | |
| - | [[Category: Rhodocytin]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
CLC1B_HUMAN
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nagae M, Morita-Matsumoto K, Kato M, Kaneko MK, Kato Y, Yamaguchi Y. A Platform of C-type Lectin-like Receptor CLEC-2 for Binding O-Glycosylated Podoplanin and Nonglycosylated Rhodocytin. Structure. 2014 Dec 2;22(12):1711-21. doi: 10.1016/j.str.2014.09.009. Epub 2014, Nov 6. PMID:25458834 doi:http://dx.doi.org/10.1016/j.str.2014.09.009
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