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| <StructureSection load='6psf' size='340' side='right'caption='[[6psf]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='6psf' size='340' side='right'caption='[[6psf]], [[Resolution|resolution]] 3.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6psf]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Rhinovirus_c Rhinovirus c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PSF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PSF FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6psf]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rhinovirus_C Rhinovirus C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PSF FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDHR3, CDH28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6psf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6psf OCA], [http://pdbe.org/6psf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6psf RCSB], [http://www.ebi.ac.uk/pdbsum/6psf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6psf 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=6psf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6psf OCA], [https://pdbe.org/6psf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6psf RCSB], [https://www.ebi.ac.uk/pdbsum/6psf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6psf ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Disease ==
| |
| [[http://www.uniprot.org/uniprot/CDHR3_HUMAN CDHR3_HUMAN]] Asthma susceptibility may be associated with variations affecting the gene represented in this entry in early childhood asthma with severe exacerbations occurring between 2 and 6 years of age.<ref>PMID:24241537</ref>
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| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/CDHR3_HUMAN CDHR3_HUMAN]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. (Microbial infection) Acts as a receptor for rhinovirus C.<ref>PMID:25848009</ref> | | [https://www.uniprot.org/uniprot/E5D8F2_9ENTO E5D8F2_9ENTO] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
| |
| Infection by Rhinovirus-C (RV-C), a species of Picornaviridae Enterovirus, is strongly associated with childhood asthma exacerbations. Cellular binding and entry by all RV-C, which trigger these episodes, is mediated by the first extracellular domain (EC1) of cadherin-related protein 3 (CDHR3), a surface cadherin-like protein expressed primarily on the apical surfaces of ciliated airway epithelial cells. Although recombinant EC1 is a potent inhibitor of viral infection, there is no molecular description of this protein or its binding site on RV-C. Here we present cryo-electron microscopy (EM) data resolving the EC1 and EC1+2 domains of human CDHR3 complexed with viral isolate C15a. Structure-suggested residues contributing to required interfaces on both EC1 and C15a were probed and identified by mutagenesis studies with four different RV-C genotypes. In contrast to most other rhinoviruses, which bind intercellular adhesion molecule 1 receptors via a capsid protein VP1-specific fivefold canyon feature, the CDHR3 EC1 contacts C15a, and presumably all RV-Cs, in a unique cohesive footprint near the threefold vertex, encompassing residues primarily from viral protein VP3, but also from VP1 and VP2. The EC1+2 footprint on C15a is similar to that of EC1 alone but shows that steric hindrance imposed by EC2 would likely prevent multiprotein binding by the native receptor at any singular threefold vertex. Definition of the molecular interface between the RV-Cs and their receptors provides new avenues that can be explored for potential antiviral therapies.
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| Cryo-EM structure of rhinovirus C15a bound to its cadherin-related protein 3 receptor.,Sun Y, Watters K, Hill MG, Fang Q, Liu Y, Kuhn RJ, Klose T, Rossmann MG, Palmenberg AC Proc Natl Acad Sci U S A. 2020 Mar 24;117(12):6784-6791. doi:, 10.1073/pnas.1921640117. Epub 2020 Mar 9. PMID:32152109<ref>PMID:32152109</ref>
| | ==See Also== |
| | | *[[Human rhinovirus|Human rhinovirus]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6psf" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Human]] | | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Rhinovirus c]] | | [[Category: Rhinovirus C]] |
| [[Category: Klose, T]] | | [[Category: Klose T]] |
| [[Category: Palmenberg, A C]] | | [[Category: Palmenberg AC]] |
| [[Category: Sun, Y]] | | [[Category: Sun Y]] |
| [[Category: Watters, K]] | | [[Category: Watters K]] |
| [[Category: Cadherin]]
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| [[Category: Receptor]]
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| [[Category: Virus-cell adhesion complex]]
| |