| First Author | Wang R | Year | 2012 |
| Journal | Proc Natl Acad Sci U S A | Volume | 109 |
| Issue | 51 | Pages | E3578-87 |
| PubMed ID | 23169621 | Mgi Jnum | J:192334 |
| Mgi Id | MGI:5464941 | Doi | 10.1073/pnas.1214088109 |
| Citation | Wang R, et al. (2012) Structural basis of mouse cytomegalovirus m152/gp40 interaction with RAE1gamma reveals a paradigm for MHC/MHC interaction in immune evasion. Proc Natl Acad Sci U S A 109(51):E3578-87 |
| abstractText | Natural killer (NK) cells are activated by engagement of the NKG2D receptor with ligands on target cells stressed by infection or tumorigenesis. Several human and rodent cytomegalovirus (CMV) immunoevasins down-regulate surface expression of NKG2D ligands. The mouse CMV MHC class I (MHC-I)-like m152/gp40 glycoprotein down-regulates retinoic acid early inducible-1 (RAE1) NKG2D ligands as well as host MHC-I. Here we describe the crystal structure of an m152/RAE1gamma complex and confirm the intermolecular contacts by mutagenesis. m152 interacts in a pincer-like manner with two sites on the alpha1 and alpha2 helices of RAE1 reminiscent of the NKG2D interaction with RAE1. This structure of an MHC-I-like immunoevasin/MHC-I-like ligand complex explains the binding specificity of m152 for RAE1 and allows modeling of the interaction of m152 with classical MHC-I and of related viral immunoevasins. |
