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| | ==Crystal Structure of extracellular domain of mouse NKR-P1A== | | ==Crystal Structure of extracellular domain of mouse NKR-P1A== |
| - | <StructureSection load='3m9z' size='340' side='right' caption='[[3m9z]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3m9z' size='340' side='right'caption='[[3m9z]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3m9z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M9Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3m9z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M9Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e87|1e87]], [[1egg|1egg]], [[1ixx|1ixx]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Klrb1a, Ly55, Ly55a, Nkrp1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3m9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9z OCA], [https://pdbe.org/3m9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m9z RCSB], [https://www.ebi.ac.uk/pdbsum/3m9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m9z 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=3m9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m9z RCSB], [http://www.ebi.ac.uk/pdbsum/3m9z PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KLRBA_MOUSE KLRBA_MOUSE]] Plays a stimulatory role on natural killer (NK) cell cytotoxicity.<ref>PMID:16751398</ref> | + | [https://www.uniprot.org/uniprot/KLRBA_MOUSE KLRBA_MOUSE] Plays a stimulatory role on natural killer (NK) cell cytotoxicity.<ref>PMID:16751398</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 3m9z" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Bezouska, K]] | + | [[Category: Mus musculus]] |
| - | [[Category: Dohnalek, J]] | + | [[Category: Bezouska K]] |
| - | [[Category: Hasek, J]] | + | [[Category: Dohnalek J]] |
| - | [[Category: Kolenko, P]] | + | [[Category: Hasek J]] |
| - | [[Category: Rozbesky, D]] | + | [[Category: Kolenko P]] |
| - | [[Category: C-type lectin-like domain]]
| + | [[Category: Rozbesky D]] |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Domain swapping]]
| + | |
| - | [[Category: Natural killer cell receptor]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Transmembrane protein]]
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| Structural highlights
Function
KLRBA_MOUSE Plays a stimulatory role on natural killer (NK) cell cytotoxicity.[1]
Publication Abstract from PubMed
Receptors belonging to NKR-P1 family and their specific Clr ligands form an alternative missing self recognition system critical in immunity against tumors and viruses, elimination of tumor cells subjected to genotoxic stress, activation of T cell dependent immune response, and hypertension. The three-dimensional structure of the extracellular domain of the mouse natural killer (NK) cell receptor mNKR-P1Aex has been determined by X-ray diffraction. The core of the C-type lectin domain (CTLD) is homologous to the other CTLD receptors whereas one quarter of the domain forms an extended loop interacting tightly with a neighboring loop in the crystal. This domain swapping mechanism results in a compact interaction interface. A second dimerization interface resembles the known arrangement of other CTLD NK receptors. A functional dimeric form of the receptor is suggested, with the loop, evolutionarily conserved within this family, proposed to participate in interactions with ligands.
Molecular architecture of mouse activating NKR-P1 receptors.,Kolenko P, Rozbesky D, Vanek O, Kopecky V Jr, Hofbauerova K, Novak P, Pompach P, Hasek J, Skalova T, Bezouska K, Dohnalek J J Struct Biol. 2011 Sep;175(3):434-41. doi: 10.1016/j.jsb.2011.05.001. Epub 2011 , May 12. PMID:21600988[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carlyle JR, Mesci A, Ljutic B, Belanger S, Tai LH, Rousselle E, Troke AD, Proteau MF, Makrigiannis AP. Molecular and genetic basis for strain-dependent NK1.1 alloreactivity of mouse NK cells. J Immunol. 2006 Jun 15;176(12):7511-24. PMID:16751398
- ↑ Kolenko P, Rozbesky D, Vanek O, Kopecky V Jr, Hofbauerova K, Novak P, Pompach P, Hasek J, Skalova T, Bezouska K, Dohnalek J. Molecular architecture of mouse activating NKR-P1 receptors. J Struct Biol. 2011 Sep;175(3):434-41. doi: 10.1016/j.jsb.2011.05.001. Epub 2011 , May 12. PMID:21600988 doi:http://dx.doi.org/10.1016/j.jsb.2011.05.001
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