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| | <StructureSection load='4wol' size='340' side='right'caption='[[4wol]], [[Resolution|resolution]] 1.77Å' scene=''> | | <StructureSection load='4wol' size='340' side='right'caption='[[4wol]], [[Resolution|resolution]] 1.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wol]] is a 3 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=4WOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WOL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wol]] is a 3 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=4WOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WOL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wo1|4wo1]], [[2l34|2l34]], [[2l35|2l35]]</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=4wol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wol OCA], [https://pdbe.org/4wol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wol RCSB], [https://www.ebi.ac.uk/pdbsum/4wol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wol ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TYROBP, DAP12, KARAP ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wol OCA], [http://pdbe.org/4wol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wol RCSB], [http://www.ebi.ac.uk/pdbsum/4wol PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wol ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/TYOBP_HUMAN TYOBP_HUMAN]] Nasu-Hakola disease. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/TYOBP_HUMAN TYOBP_HUMAN] Nasu-Hakola disease. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TYOBP_HUMAN TYOBP_HUMAN]] Non-covalently associates with activating receptors of the CD300 family. Cross-linking of CD300-TYROBP complexes results in cellular activation. Involved for instance in neutrophil activation mediated by integrin. | + | [https://www.uniprot.org/uniprot/TYOBP_HUMAN TYOBP_HUMAN] Non-covalently associates with activating receptors of the CD300 family. Cross-linking of CD300-TYROBP complexes results in cellular activation. Involved for instance in neutrophil activation mediated by integrin. |
| | <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: Call, M E]] | + | [[Category: Call ME]] |
| - | [[Category: Call, M J]] | + | [[Category: Call MJ]] |
| - | [[Category: Knoblich, K]] | + | [[Category: Knoblich K]] |
| - | [[Category: Alpha-helix transmembrane signalling]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Disease
TYOBP_HUMAN Nasu-Hakola disease. The disease is caused by mutations affecting the gene represented in this entry.
Function
TYOBP_HUMAN Non-covalently associates with activating receptors of the CD300 family. Cross-linking of CD300-TYROBP complexes results in cellular activation. Involved for instance in neutrophil activation mediated by integrin.
Publication Abstract from PubMed
The membrane-spanning alpha helices of single-pass receptors play crucial roles in stabilizing oligomeric structures and transducing biochemical signals across the membrane. Probing intermolecular transmembrane interactions in single-pass receptors presents unique challenges, reflected in a gross underrepresentation of their membrane-embedded domains in structural databases. Here, we present two high-resolution structures of transmembrane assemblies from a eukaryotic single-pass protein crystallized in a lipidic membrane environment. Trimeric and tetrameric structures of the immunoreceptor signaling module DAP12, determined to 1.77-A and 2.14-A resolution, respectively, are organized by the same polar surfaces that govern intramembrane assembly with client receptors. We demonstrate that, in addition to the well-studied dimeric form, these trimeric and tetrameric structures are made in cells, and their formation is competitive with receptor association in the ER. The polar transmembrane sequences therefore act as primary determinants of oligomerization specificity through interplay between charge shielding and sequestration of polar surfaces within helix interfaces.
Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly.,Knoblich K, Park S, Lutfi M, van 't Hag L, Conn CE, Seabrook SA, Newman J, Czabotar PE, Im W, Call ME, Call MJ Cell Rep. 2015 May 26;11(8):1184-92. doi: 10.1016/j.celrep.2015.04.045. Epub 2015, May 14. PMID:25981043[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Knoblich K, Park S, Lutfi M, van 't Hag L, Conn CE, Seabrook SA, Newman J, Czabotar PE, Im W, Call ME, Call MJ. Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly. Cell Rep. 2015 May 26;11(8):1184-92. doi: 10.1016/j.celrep.2015.04.045. Epub 2015, May 14. PMID:25981043 doi:http://dx.doi.org/10.1016/j.celrep.2015.04.045
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