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| <StructureSection load='5vcl' size='340' side='right'caption='[[5vcl]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='5vcl' size='340' side='right'caption='[[5vcl]], [[Resolution|resolution]] 2.05Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5vcl]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VCL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5VCL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vcl]] 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=5VCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VCL FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.05Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vj6|3vj6]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5vcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vcl OCA], [http://pdbe.org/5vcl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vcl RCSB], [http://www.ebi.ac.uk/pdbsum/5vcl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vcl ProSAT]</span></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=5vcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vcl OCA], [https://pdbe.org/5vcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vcl RCSB], [https://www.ebi.ac.uk/pdbsum/5vcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vcl ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/HA1L_MOUSE HA1L_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/HA1L_MOUSE HA1L_MOUSE] Involved in the presentation of foreign 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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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Ying, G]] | + | [[Category: Mus musculus]] |
- | [[Category: Zajonc, D M]] | + | [[Category: Ying G]] |
- | [[Category: Antigen-presentation]] | + | [[Category: Zajonc DM]] |
- | [[Category: Immune system]]
| + | |
- | [[Category: Mhc]]
| + | |
| Structural highlights
Function
HA1L_MOUSE Involved in the presentation of foreign antigens to the immune system.
Publication Abstract from PubMed
Qa-1 is a non-classical Major Histocompatibility (MHC) class I molecule that generally presents hydrophobic peptides including Qdm derived from the leader sequence of classical MHC I molecules for immune surveillance by NK cells. Qa-1 bound peptides derived from the TCR Vbeta8.2 of activated T cells also activates CD8+ regulatory T cells to control autoimmunity and maintain self-tolerance. Four allotypes of Qa-1 (Qa-1a-d) are expressed that are highly conserved in sequence but have several variations that could affect peptide binding to Qa-1 or TCR recognition. Here, we determined the structure of Qa-1a with bound Qdm peptide. While the overall structure is very similar to that of Qa-1b, there are several amino acid differences around the peptide binding platform that could affect TCR recognition. Most notably, two amino acid substitutions are found in the pocket P2, which binds the anchor residue Met2 of the Qdm peptide. These residues affect both the size and shape of the binding pocket, as well as affect the charge at physiologic pH, suggesting Qa-1a and Qa-1b could present slightly distinct peptide reservoirs, which could presumably be recognized by different populations of CD8+ T cells.
Crystal structure of Qa-1a with bound Qa-1 determinant modifier peptide.,Ying G, Wang J, Kumar V, Zajonc DM PLoS One. 2017 Aug 2;12(8):e0182296. doi: 10.1371/journal.pone.0182296., eCollection 2017. PMID:28767728[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ying G, Wang J, Kumar V, Zajonc DM. Crystal structure of Qa-1a with bound Qa-1 determinant modifier peptide. PLoS One. 2017 Aug 2;12(8):e0182296. doi: 10.1371/journal.pone.0182296., eCollection 2017. PMID:28767728 doi:http://dx.doi.org/10.1371/journal.pone.0182296
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