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| | <StructureSection load='4pbp' size='340' side='right'caption='[[4pbp]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='4pbp' size='340' side='right'caption='[[4pbp]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pbp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PBP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PBP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pbp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PBP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.648Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pbo|4pbo]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">crp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</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=4pbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pbp OCA], [https://pdbe.org/4pbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pbp RCSB], [https://www.ebi.ac.uk/pdbsum/4pbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pbp ProSAT]</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=4pbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pbp OCA], [http://pdbe.org/4pbp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pbp RCSB], [http://www.ebi.ac.uk/pdbsum/4pbp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pbp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CRP_DANRE CRP_DANRE] Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis, and complement fixation through its calcium-dependent binding to phosphorylcholine.[UniProtKB:P19094] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4pbp" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4pbp" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[C-reactive protein|C-reactive protein]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brachidanio rerio]] | + | [[Category: Danio rerio]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, R]] | + | [[Category: Chen R]] |
| - | [[Category: George, F G]] | + | [[Category: George FG]] |
| - | [[Category: Qi, J X]] | + | [[Category: Qi JX]] |
| - | [[Category: Xia, C]] | + | [[Category: Xia C]] |
| - | [[Category: Acute phase protein]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Pentraxin]]
| + | |
| Structural highlights
Function
CRP_DANRE Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis, and complement fixation through its calcium-dependent binding to phosphorylcholine.[UniProtKB:P19094]
Publication Abstract from PubMed
Short-chain pentraxins (PTXs), including CRP and SAP, are innate pattern recognition receptors that play vital roles in the recognition and elimination of various pathogenic bacteria by triggering the classical complement pathway through C1q. Similar to antibodies, pentraxins can also activate opsonisation and phagocytosis by interacting with Fc receptors (FcRs). Various structural studies on human PTXs have been performed, but there are no reports about the crystal structure of bony fish pentraxins. Here, the crystal structures of zebrafish PTX (Dare-PTX-Ca and Dare-PTX) are presented. Both Dare-PTX-Ca and Dare-PTX are cyclic trimers, which are new forms of crystallised pentraxins. The structures reveal that the ligand-binding pocket (LBP) in the recognition face of Dare-PTX is deep and narrow. Homology modelling shows that LBPs from different Dare-PTX loci differ in shape, reflecting their specific recognition abilities. Furthermore, in comparison with the structure of hCPR, a new C1q binding mode was identified in Dare-PTX. In addition, the FcR-binding sites of hSAP are partially conserved in Dare-PTX. These results will shed light on the understanding of a primitive PTX in bony fish, which evolved approximately 450 million years ago.
Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces.,Chen R, Qi J, Yuan H, Wu Y, Hu W, Xia C J Struct Biol. 2015 Mar;189(3):259-68. doi: 10.1016/j.jsb.2015.01.001. Epub 2015 , Jan 13. PMID:25592778[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen R, Qi J, Yuan H, Wu Y, Hu W, Xia C. Crystal structures for short-chain pentraxin from zebrafish demonstrate a cyclic trimer with new recognition and effector faces. J Struct Biol. 2015 Mar;189(3):259-68. doi: 10.1016/j.jsb.2015.01.001. Epub 2015 , Jan 13. PMID:25592778 doi:http://dx.doi.org/10.1016/j.jsb.2015.01.001
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