4G59

Crystal structure of the murine cytomegalovirus MHC-I homolog m152 with ligand RAE-1 gamma

Summary for 4G59

• Entry DOI: 10.2210/pdb4g59/pdb
• Descriptor: Retinoic acid early-inducible protein 1-gamma, M152 protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: mhc-i fold, immunoevasion, stress induced ligand, immune system
• Biological source: Mus musculus (mouse); More
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: O08604
• Total number of polymer chains: 4
• Total formula weight: 120729.28

Authors

Wang, R.,Natarajan, K.,Margulies, D.H. (deposition date: 2012-07-17, release date: 2012-12-19, Last modification date: 2024-11-20)

Primary citation

Wang, R.,Natarajan, K.,Revilleza, M.J.,Boyd, L.F.,Zhi, L.,Zhao, H.,Robinson, H.,Margulies, D.H.
Structural basis of mouse cytomegalovirus m152/gp40 interaction with RAE1gamma reveals a paradigm for MHC/MHC interaction in immune evasion.
Proc.Natl.Acad.Sci.USA, 109:E3578-E3587, 2012

PubMed Abstract: 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/RAE1γ complex and confirm the intermolecular contacts by mutagenesis. m152 interacts in a pincer-like manner with two sites on the α1 and α2 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.

PubMed: 23169621
DOI: 10.1073/pnas.1214088109

Experimental method

X-RAY DIFFRACTION (2.44 Å)