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| | <StructureSection load='5eiv' size='340' side='right'caption='[[5eiv]], [[Resolution|resolution]] 2.41Å' scene=''> | | <StructureSection load='5eiv' size='340' side='right'caption='[[5eiv]], [[Resolution|resolution]] 2.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5eiv]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EIV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EIV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5eiv]] is a 11 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=5EIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EIV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</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=5eiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eiv OCA], [https://pdbe.org/5eiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eiv RCSB], [https://www.ebi.ac.uk/pdbsum/5eiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eiv ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OSCAR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5eiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eiv OCA], [http://pdbe.org/5eiv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eiv RCSB], [http://www.ebi.ac.uk/pdbsum/5eiv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eiv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OSCAR_HUMAN OSCAR_HUMAN]] Regulator of osteoclastogenesis which plays an important bone-specific function in osteoclast differentiation. | + | [https://www.uniprot.org/uniprot/OSCAR_HUMAN OSCAR_HUMAN] Regulator of osteoclastogenesis which plays an important bone-specific function in osteoclast differentiation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bihan, D]] | + | [[Category: Bihan D]] |
| - | [[Category: Blaszczyk, M]] | + | [[Category: Blaszczyk M]] |
| - | [[Category: Chirgadze, D]] | + | [[Category: Chirgadze D]] |
| - | [[Category: Farndale, R W]] | + | [[Category: Farndale RW]] |
| - | [[Category: Zhou, L]] | + | [[Category: Zhou L]] |
| - | [[Category: Collagen]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Immunoglobulin]]
| + | |
| - | [[Category: Oscar]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Triple helix]]
| + | |
| Structural highlights
5eiv is a 11 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
OSCAR_HUMAN Regulator of osteoclastogenesis which plays an important bone-specific function in osteoclast differentiation.
Publication Abstract from PubMed
The Osteoclast-associated receptor (OSCAR) is a collagen-binding immune receptor with important roles in dendritic cell maturation and activation of inflammatory monocytes as well as in osteoclastogenesis. The crystal structure of the OSCAR ectodomain is presented, both free and in complex with a consensus triple-helical peptide (THP). The structures revealed a collagen-binding site in each Ig-like domain (D1 and D2). The THP binds near a hypothetical collagen-binding groove in D1, but a more extensive interaction with D2 is facilitated by the unusually wide D1-D2 inter-domain angle in OSCAR. Direct binding assays, combined with site-directed mutagenesis, confirm that the primary collagen-binding site in OSCAR resides in D2, in marked contrast to the related collagen receptors, GPVI and LAIR-1. Monomeric OSCAR D1D2 binds to the consensus THP with a KD of 28 muM measured in solution, but shows a higher affinity (KD 1.5 muM) when binding to a solid-phase THP, most likely due to an avidity effect. These data suggest a two-stage model for the interaction of OSCAR with a collagen fibril, with transient, low-affinity interactions initiated by the membrane-distal D1, followed by firm adhesion to the primary binding site in D2.
Structural basis for collagen recognition by the immune receptor OSCAR.,Zhou L, Hinerman JM, Blaszczyk M, Miller JL, Conrady DG, Barrow AD, Chirgadze DY, Bihan D, Farndale RW, Herr AB Blood. 2015 Nov 9. pii: blood-2015-08-667055. PMID:26552697[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhou L, Hinerman JM, Blaszczyk M, Miller JL, Conrady DG, Barrow AD, Chirgadze DY, Bihan D, Farndale RW, Herr AB. Structural basis for collagen recognition by the immune receptor OSCAR. Blood. 2015 Nov 9. pii: blood-2015-08-667055. PMID:26552697 doi:http://dx.doi.org/10.1182/blood-2015-08-667055
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