7p4b: Difference between revisions
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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=7p4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p4b OCA], [https://pdbe.org/7p4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p4b RCSB], [https://www.ebi.ac.uk/pdbsum/7p4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p4b 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=7p4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p4b OCA], [https://pdbe.org/7p4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p4b RCSB], [https://www.ebi.ac.uk/pdbsum/7p4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p4b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ | [https://www.uniprot.org/uniprot/HLAE_HUMAN HLAE_HUMAN] Preferably binds to a peptide derived from the signal sequence of most HLA-A, -B, -C and -G molecules. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 12:32, 9 October 2024
HLA-E*01:03 in complex with IL9HLA-E*01:03 in complex with IL9
Structural highlights
FunctionHLAE_HUMAN Preferably binds to a peptide derived from the signal sequence of most HLA-A, -B, -C and -G molecules. Publication Abstract from PubMedMHC-E regulates NK cells by displaying MHC class Ia signal peptides (VL9) to NKG2A:CD94 receptors. MHC-E can also present sequence-diverse, lower-affinity, pathogen-derived peptides to T cell receptors (TCRs) on CD8(+) T cells. To understand these affinity differences, human MHC-E (HLA-E)-VL9 versus pathogen-derived peptide structures are compared. Small-angle X-ray scatter (SAXS) measures biophysical parameters in solution, allowing comparison with crystal structures. For HLA-E-VL9, there is concordance between SAXS and crystal parameters. In contrast, HLA-E-bound pathogen-derived peptides produce larger SAXS dimensions that reduce to their crystallographic dimensions only when excess peptide is supplied. Further crystallographic analysis demonstrates three amino acids, exclusive to MHC-E, that not only position VL9 close to the alpha2 helix, but also allow non-VL9 peptide binding with re-configuration of a key TCR-interacting alpha2 region. Thus, non-VL9-bound peptides introduce an alternative peptide-binding motif and surface recognition landscape, providing a likely basis for VL9- and non-VL9-HLA-E immune discrimination. Primary and secondary functions of HLA-E are determined by stability and conformation of the peptide-bound complexes.,Walters LC, Rozbesky D, Harlos K, Quastel M, Sun H, Springer S, Rambo RP, Mohammed F, Jones EY, McMichael AJ, Gillespie GM Cell Rep. 2022 Jun 14;39(11):110959. doi: 10.1016/j.celrep.2022.110959. PMID:35705051[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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