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==Murine CD94-NKG2A receptor in complex with Qa-1b presenting | ==Murine CD94-NKG2A receptor in complex with Qa-1b presenting AMAPRTLLL== | ||
<StructureSection load='8umo' size='340' side='right'caption='[[8umo]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='8umo' size='340' side='right'caption='[[8umo]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8umo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8umo OCA], [https://pdbe.org/8umo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8umo RCSB], [https://www.ebi.ac.uk/pdbsum/8umo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8umo 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=8umo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8umo OCA], [https://pdbe.org/8umo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8umo RCSB], [https://www.ebi.ac.uk/pdbsum/8umo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8umo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | |||
The heterodimeric natural killer cells antigen CD94 (CD94)-NKG2-A/NKG2-B type II integral membrane protein (NKG2A) receptor family expressed on human and mouse natural killer (NK) cells monitors global major histocompatibility complex (MHC) class I cell surface expression levels through binding to MHC class Ia-derived leader sequence peptides presented by HLA class I histocompatibility antigen, alpha chain E (HLA-E; in humans) or H-2 class I histocompatibility antigen, D-37 (Qa-1(b); in mice). Although the molecular basis underpinning human CD94-NKG2A recognition of HLA-E is known, the equivalent interaction in the murine setting is not. By determining the high-resolution crystal structure of murine CD94-NKG2A in complex with Qa-1(b) presenting the Qa-1 determinant modifier peptide (QDM), we resolved the mode of binding. Compared to the human homologue, the murine CD94-NKG2A-Qa-1(b)-QDM displayed alterations in the distribution of interactions across CD94 and NKG2A subunits that coincide with differences in electrostatic complementarity of the ternary complex and the lack of cross-species reactivity. Nevertheless, we show that Qa-1b could be modified through W65R + N73I mutations to mimic HLA-E, facilitating binding with both human and murine CD94-NKG2A. These data underscore human and murine CD94-NKG2A cross-species heterogeneity and provide a foundation for humanising Qa-1b in immune system models. | |||
Structure of the murine CD94-NKG2A receptor in complex with Qa-1(b) presenting an MHC-I leader peptide.,MacLachlan BJ, Sullivan LC, Brooks AG, Rossjohn J, Vivian JP FEBS J. 2024 Apr;291(7):1530-1544. doi: 10.1111/febs.17050. Epub 2024 Jan 10. PMID:38158698<ref>PMID:38158698</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 8umo" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 12:59, 17 October 2024
Murine CD94-NKG2A receptor in complex with Qa-1b presenting AMAPRTLLLMurine CD94-NKG2A receptor in complex with Qa-1b presenting AMAPRTLLL
Structural highlights
Publication Abstract from PubMedThe heterodimeric natural killer cells antigen CD94 (CD94)-NKG2-A/NKG2-B type II integral membrane protein (NKG2A) receptor family expressed on human and mouse natural killer (NK) cells monitors global major histocompatibility complex (MHC) class I cell surface expression levels through binding to MHC class Ia-derived leader sequence peptides presented by HLA class I histocompatibility antigen, alpha chain E (HLA-E; in humans) or H-2 class I histocompatibility antigen, D-37 (Qa-1(b); in mice). Although the molecular basis underpinning human CD94-NKG2A recognition of HLA-E is known, the equivalent interaction in the murine setting is not. By determining the high-resolution crystal structure of murine CD94-NKG2A in complex with Qa-1(b) presenting the Qa-1 determinant modifier peptide (QDM), we resolved the mode of binding. Compared to the human homologue, the murine CD94-NKG2A-Qa-1(b)-QDM displayed alterations in the distribution of interactions across CD94 and NKG2A subunits that coincide with differences in electrostatic complementarity of the ternary complex and the lack of cross-species reactivity. Nevertheless, we show that Qa-1b could be modified through W65R + N73I mutations to mimic HLA-E, facilitating binding with both human and murine CD94-NKG2A. These data underscore human and murine CD94-NKG2A cross-species heterogeneity and provide a foundation for humanising Qa-1b in immune system models. Structure of the murine CD94-NKG2A receptor in complex with Qa-1(b) presenting an MHC-I leader peptide.,MacLachlan BJ, Sullivan LC, Brooks AG, Rossjohn J, Vivian JP FEBS J. 2024 Apr;291(7):1530-1544. doi: 10.1111/febs.17050. Epub 2024 Jan 10. PMID:38158698[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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