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| | <StructureSection load='5j6h' size='340' side='right'caption='[[5j6h]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5j6h' size='340' side='right'caption='[[5j6h]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5j6h]] is a 3 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=5J6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J6H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j6h]] is a 3 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=5J6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J6H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NCA:NICOTINAMIDE'>NCA</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j6g|5j6g]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NCA:NICOTINAMIDE'>NCA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-Q10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), B2m ([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=5j6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j6h OCA], [https://pdbe.org/5j6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j6h RCSB], [https://www.ebi.ac.uk/pdbsum/5j6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j6h 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=5j6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j6h OCA], [http://pdbe.org/5j6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j6h RCSB], [http://www.ebi.ac.uk/pdbsum/5j6h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j6h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HA10_MOUSE HA10_MOUSE]] Involved in the presentation of foreign antigens to the immune system. [[http://www.uniprot.org/uniprot/B2MG_MOUSE B2MG_MOUSE]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. | + | [https://www.uniprot.org/uniprot/B2MG_MOUSE B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] |
| | + | *[[MHC 3D structures|MHC 3D structures]] |
| | + | *[[MHC I 3D structures|MHC I 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Berry, R]] | + | [[Category: Berry R]] |
| - | [[Category: Rossjohn, J]] | + | [[Category: Rossjohn J]] |
| - | [[Category: Immune system]]
| + | |
| Structural highlights
Function
B2MG_MOUSE Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
Publication Abstract from PubMed
Murine Natural Killer (NK) cells are regulated by the interaction of Ly49 receptors with major histocompatibility complex class I (MHC-I) molecules. While the ligands for inhibitory Ly49 were considered to be restricted to classical MHC (MHC-Ia), we have shown that the non-classical MHC (MHC-Ib) molecule H2-M3 was a ligand for the inhibitory Ly49A. Here we establish that another MHC-Ib molecule, H2-Q10, is a bona fide ligand for the inhibitory Ly49C receptor. H2-Q10 bound to Ly49C with a lower affinity (~ 5muM) than that observed between Ly49C and MHC-Ia (H-2Kb/H-2Dd, both ~ 1muM) and this recognition could be prevented by cis interactions with H-2Kb in situ. In order to understand the molecular details underpinning Ly49/MHC-Ib recognition, we determined the crystal structures of H2-Q10 and Ly49C bound H2-Q10. Unliganded H2-Q10 adopted a classical MHC-I fold and possessed a peptide-binding groove that exhibited features similar to those found in MHC-Ia, explaining the diverse peptide-binding repertoire of H2-Q10. Ly49C bound to H2-Q10 underneath the peptide-binding platform to a region that encompassed residues from the alpha1, alpha2 and alpha3 domains, as well as the associated beta2-microglobulin subunit. This docking mode was conserved with that previously observed for Ly49C/H-2Kb. Indeed, structure-guided mutation of Ly49C indicated that Ly49C/H2-Q10 and Ly49C/H-2Kb possess similar energetic footprints focused around residues located within the Ly49C beta4-stand and L5 loop, which contact the underside of the peptide binding platform floor. Our data provides a structural basis for Ly49-MHC-Ib recognition and demonstrate that MHC-Ib represent an extended family of ligands for Ly49 molecules.
Recognition of the MHC class Ib molecule H2-Q10 by the natural killer cell receptor Ly49C.,Sullivan LC, Berry R, Sosnin N, Widjaja JM, Deuss FA, Balaji GR, LaGruta NL, Mirams M, Trapani JA, Rossjohn J, Brooks AG, Andrews DM J Biol Chem. 2016 Jul 6. pii: jbc.M116.737130. PMID:27385590[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sullivan LC, Berry R, Sosnin N, Widjaja JM, Deuss FA, Balaji GR, LaGruta NL, Mirams M, Trapani JA, Rossjohn J, Brooks AG, Andrews DM. Recognition of the MHC class Ib molecule H2-Q10 by the natural killer cell receptor Ly49C. J Biol Chem. 2016 Jul 6. pii: jbc.M116.737130. PMID:27385590 doi:http://dx.doi.org/10.1074/jbc.M116.737130
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