ArticleStructure (London, England : 1993)2014
The structure of mouse cytomegalovirus m04 protein obtained from sparse NMR data reveals a conserved fold of the m02-m06 viral immune modulator family.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 24 citations in OpenAlex.
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- Modulation of innate and adaptive immunity by cytomegaloviruses.Nature reviews. Immunology · 2020Review
- Positive Role of the MHC Class-I Antigen Presentation Regulator m04/gp34 of Murine Cytomegalovirus in Antiviral Protection by CD8 T Cells.Frontiers in cellular and infection microbiology · 2020Article
- Unraveling the structure and dynamics of the human DNAJB6b chaperone by NMR reveals insights into Hsp40-mediated proteostasis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Function of the cargo sorting dileucine motif in a cytomegalovirus immune evasion protein.Medical microbiology and immunology · 2019Article
- Combining Evolutionary Covariance and NMR Data for Protein Structure Determination.Methods in enzymology · 2019Article
- Sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction of both non-uniformly sampled and conventional NMR data.Journal of biomolecular NMR · 2017Article
- Critical assessment of methods of protein structure prediction: Progress and new directions in round XI.Proteins · 2016Article
- A Novel MHC-I Surface Targeted for Binding by the MCMV m06 Immunoevasin Revealed by Solution NMR.The Journal of biological chemistry · 2015Article
- A hybrid NMR/SAXS-based approach for discriminating oligomeric protein interfaces using Rosetta.Proteins · 2015Article
- NMR structure determination of the protein NP_344798.1 as the first representative of Pfam PF06042.Journal of biomolecular NMR · 2015Article
- J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.Journal of biomolecular NMR · 2015Article
- Less is more: structures of difficult targets with minimal constraints.Structure (London, England : 1993) · 2014Article
- Chemical shift-based methods in NMR structure determination.Progress in nuclear magnetic resonance spectroscopyReview
- A Hybrid Approach for Protein Structure Determination Combining Sparse NMR with Evolutionary Coupling Sequence Data.Advances in experimental medicine and biologyReview
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7 authors at 3 institutions in 1 country.
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Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.