Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6GH4

HLA-E*01:03 in complex with the Mtb44 peptide variant: Mtb44*P2-Gln.

Summary for 6GH4
Entry DOI10.2210/pdb6gh4/pdb
DescriptorMHC class I antigen, Beta-2-microglobulin, ARG-GLN-PRO-ALA-LYS-ALA-PRO-LEU-LEU, ... (6 entities in total)
Functional Keywordscomplex, histocompatibility antigen, immune system
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains12
Total formula weight178627.00
Authors
Walters, L.C.,Gillespie, G.M.,McMichael, A.J.,Rozbesky, D.,Jones, E.Y.,Harlos, K. (deposition date: 2018-05-04, release date: 2018-08-08, Last modification date: 2024-10-23)
Primary citationWalters, L.C.,Harlos, K.,Brackenridge, S.,Rozbesky, D.,Barrett, J.R.,Jain, V.,Walter, T.S.,O'Callaghan, C.A.,Borrow, P.,Toebes, M.,Hansen, S.G.,Sacha, J.,Abdulhaqq, S.,Greene, J.M.,Fruh, K.,Marshall, E.,Picker, L.J.,Jones, E.Y.,McMichael, A.J.,Gillespie, G.M.
Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding.
Nat Commun, 9:3137-3137, 2018
Cited by
PubMed Abstract: Through major histocompatibility complex class Ia leader sequence-derived (VL9) peptide binding and CD94/NKG2 receptor engagement, human leucocyte antigen E (HLA-E) reports cellular health to NK cells. Previous studies demonstrated a strong bias for VL9 binding by HLA-E, a preference subsequently supported by structural analyses. However, Mycobacteria tuberculosis (Mtb) infection and Rhesus cytomegalovirus-vectored SIV vaccinations revealed contexts where HLA-E and the rhesus homologue, Mamu-E, presented diverse pathogen-derived peptides to CD8 T cells, respectively. Here we present crystal structures of HLA-E in complex with HIV and Mtb-derived peptides. We show that despite the presence of preferred primary anchor residues, HLA-E-bound peptides can adopt alternative conformations within the peptide binding groove. Furthermore, combined structural and mutagenesis analyses illustrate a greater tolerance for hydrophobic and polar residues in the primary pockets than previously appreciated. Finally, biochemical studies reveal HLA-E peptide binding and exchange characteristics with potential relevance to its alternative antigen presenting function in vivo.
PubMed: 30087334
DOI: 10.1038/s41467-018-05459-z
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.16 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon