The structure of mouse cytomegalovirus m04 protein obtained from sparse NMR data reveals a conserved fold of the m02-m06 viral immune modulator family

Structure. 2014 Sep 2;22(9):1263-1273. doi: 10.1016/j.str.2014.05.018. Epub 2014 Aug 7.


Immunoevasins are key proteins used by viruses to subvert host immune responses. Determining their high-resolution structures is key to understanding virus-host interactions toward the design of vaccines and other antiviral therapies. Mouse cytomegalovirus encodes a unique set of immunoevasins, the m02-m06 family, that modulates major histocompatibility complex class I (MHC-I) antigen presentation to CD8+ T cells and natural killer cells. Notwithstanding the large number of genetic and functional studies, the structural biology of immunoevasins remains incompletely understood, largely because of crystallization bottlenecks. Here we implement a technology using sparse nuclear magnetic resonance data and integrative Rosetta modeling to determine the structure of the m04/gp34 immunoevasin extracellular domain. The structure reveals a β fold that is representative of the m02-m06 family of viral proteins, several of which are known to bind MHC-I molecules and interfere with antigen presentation, suggesting its role as a diversified immune regulation module.

Publication types

  • Research Support, N.I.H., Intramural

MeSH terms

  • Amino Acid Sequence
  • Carrier Proteins / chemistry*
  • Conserved Sequence
  • Glycoproteins / chemistry*
  • Histocompatibility Antigens Class I / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Muromegalovirus / chemistry
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Viral Proteins / chemistry*


  • Carrier Proteins
  • Glycoproteins
  • Histocompatibility Antigens Class I
  • Viral Proteins
  • gp34 protein, cytomegalovirus

Associated data

  • PDB/2MIZ