6e7d
From Proteopedia
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==Structure of the inhibitory NKR-P1B receptor bound to the host-encoded ligand, Clr-b== | ==Structure of the inhibitory NKR-P1B receptor bound to the host-encoded ligand, Clr-b== | ||
| - | <StructureSection load='6e7d' size='340' side='right' caption='[[6e7d]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='6e7d' size='340' side='right'caption='[[6e7d]], [[Resolution|resolution]] 2.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6e7d]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E7D OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6e7d]] is a 24 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=6E7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E7D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.9Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6e7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e7d OCA], [https://pdbe.org/6e7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e7d RCSB], [https://www.ebi.ac.uk/pdbsum/6e7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e7d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CLC2D_MOUSE CLC2D_MOUSE] Receptor for KLRB1B that protects target cells against natural killer cell-mediated lysis (PubMed:14990792, PubMed:16751398). Inhibits osteoclast formation (PubMed:11278931, PubMed:12374791). Binds high molecular weight sulfated glycosaminoglycans (PubMed:15123656).<ref>PMID:11278931</ref> <ref>PMID:12374791</ref> <ref>PMID:14990792</ref> <ref>PMID:15123656</ref> <ref>PMID:16751398</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The interaction between natural killer (NK) cell inhibitory receptors and their cognate ligands constitutes a key mechanism by which healthy tissues are protected from NK cell-mediated lysis. However, self-ligand recognition remains poorly understood within the prototypical NKR-P1 receptor family. Here we report the structure of the inhibitory NKR-P1B receptor bound to its cognate host ligand, Clr-b. NKR-P1B and Clr-b interact via a head-to-head docking mode through an interface that includes a large array of polar interactions. NKR-P1B:Clr-b recognition is extremely sensitive to mutations at the heterodimeric interface, with most mutations severely impacting both Clr-b binding and NKR-P1B receptor function to implicate a low affinity interaction. Within the structure, two NKR-P1B:Clr-b complexes are cross-linked by a non-classic NKR-P1B homodimer, and the disruption of homodimer formation abrogates Clr-b recognition. These data provide an insight into a fundamental missing-self recognition system and suggest an avidity-based mechanism underpins NKR-P1B receptor function. | ||
| + | |||
| + | Recognition of host Clr-b by the inhibitory NKR-P1B receptor provides a basis for missing-self recognition.,Balaji GR, Aguilar OA, Tanaka M, Shingu-Vazquez MA, Fu Z, Gully BS, Lanier LL, Carlyle JR, Rossjohn J, Berry R Nat Commun. 2018 Nov 5;9(1):4623. doi: 10.1038/s41467-018-06989-2. PMID:30397201<ref>PMID:30397201</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6e7d" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: | + | [[Category: Balaji GR]] |
| - | [[Category: | + | [[Category: Berry R]] |
| - | [[Category: | + | [[Category: Rossjohn J]] |
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| - | + | ||
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Current revision
Structure of the inhibitory NKR-P1B receptor bound to the host-encoded ligand, Clr-b
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