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PDBsum entry 2esv

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Immune system PDB id
2esv
Contents
Protein chains
268 a.a.
100 a.a.
199 a.a.
240 a.a.
Ligands
VAL-MET-ALA-PRO-
ARG-THR-LEU-ILE-
LEU
Metals
IOD ×5
Waters ×185

References listed in PDB file
Key reference
Title Structural basis for a major histocompatibility complex class ib-Restricted t cell response.
Authors H.L.Hoare, L.C.Sullivan, G.Pietra, C.S.Clements, E.J.Lee, L.K.Ely, T.Beddoe, M.Falco, L.Kjer-Nielsen, H.H.Reid, J.Mccluskey, L.Moretta, J.Rossjohn, A.G.Brooks.
Ref. Nat Immunol, 2006, 7, 256-264. [DOI no: 10.1038/ni1312]
PubMed id 16474394
Abstract
In contrast to antigen-specific immunity orchestrated by major histocompatibility complex (MHC) class Ia molecules, the ancestrally related nonclassical MHC class Ib molecules generally mediate innate immune responses. Here we have demonstrated the structural basis by which the MHC class Ib molecule HLA-E mediates an adaptive MHC-restricted cytotoxic T lymphocyte response to human cytomegalovirus. Highly constrained by host genetics, the response showed notable fine specificity for position 8 of the viral peptide, which is the sole discriminator of self versus nonself. Despite the evolutionary divergence of MHC class Ia and class Ib molecules, the structure of the T cell receptor-MHC class Ib complex was very similar to that of conventional T cell receptor-MHC class Ia complexes. These results emphasize the evolutionary 'ambiguity' of HLA-E, which not only interacts with innate immune receptors but also has the functional capacity to mediate virus-specific cytotoxic T lymphocyte responses during adaptive immunity.
Figure 4.
Figure 4. Contribution of CDRs to the 'footprint' of the KK50.4 TCR on HLA-E-(VMAPRTLIL). The 'footprint' of the KK50.4 TCR on HLA-E-(VMAPRTLIL) (a) is compared with 'footprint' of the LC13 TCR on HLA-B8-(FLRGRAYGL) (b). Colors are as in Figure 3b.
Figure 5.
Figure 5. KK50.4 TCR-peptide interactions are dominated by the V[ ]loops. KK50.4 TCR contacts made by key peptide residues, the CD1 carbon of position 8 and atoms that make van der Waals contacts with it are orange. CDR3 , CDR1 , CDR2 and CDR3 in 'worm' format and residues in the CDR loops that make contact with the peptide are in 'ball-and-stick' (colors are as in Figure 3b.). Hydrogen bonds, dashed black lines; salt bridges, gray lines; water molecules, pink spheres.
The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Immunol (2006, 7, 256-264) copyright 2006.
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