2MIZ
Structure of the m04/gp34 mouse Cytomegalovirus Immunoevasin core domain
Summary for 2MIZ
| Entry DOI | 10.2210/pdb2miz/pdb |
| NMR Information | BMRB: 19699 |
| Descriptor | m04 immunoevasin (1 entity in total) |
| Functional Keywords | mhc class-i regulation, immunoglobulin-like fold, natural killer decoy, missing-self, rosetta modelling, ilv labelling, residual dipolar couplings, viral protein |
| Biological source | Murine cytomegalovirus (MuHV-1) |
| Total number of polymer chains | 1 |
| Total formula weight | 22799.73 |
| Authors | Sgourakis, N.G.,Natarajan, K.,Margulies, D.H.,Bax, A. (deposition date: 2013-12-21, release date: 2014-07-16, Last modification date: 2024-11-06) |
| Primary citation | Sgourakis, N.G.,Natarajan, K.,Ying, J.,Vogeli, B.,Boyd, L.F.,Margulies, D.H.,Bax, A. 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, 22:1263-1273, 2014 Cited by PubMed 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. PubMed: 25126960DOI: 10.1016/j.str.2014.05.018 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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