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PDBsum entry 2miz

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Viral protein PDB id
2miz

 

 

 

 

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Contents
Protein chain
156 a.a.
PDB id:
2miz
Name: Viral protein
Title: Structure of the m04/gp34 mouse cytomegalovirus immunoevasin core domain
Structure: M04 immunoevasin. Chain: a. Engineered: yes. Mutation: yes
Source: Murine cytomegalovirus. Muhv-1. Organism_taxid: 69156. Strain: k181. Gene: m04. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 10 models
Authors: N.G.Sgourakis,K.Natarajan,D.H.Margulies,A.Bax
Key ref: N.G.Sgourakis et al. (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. Structure, 22, 1263-1273. PubMed id: 25126960 DOI: 10.1016/j.str.2014.05.018
Date:
21-Dec-13     Release date:   16-Jul-14    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
A2Q6L0  (A2Q6L0_MUHVK) -  M04 immunoevasin (Fragment) from Murid herpesvirus 1 (strain K181)
Seq:
Struc:
266 a.a.
156 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1016/j.str.2014.05.018 Structure 22:1263-1273 (2014)
PubMed id: 25126960  
 
 
The structure of mouse cytomegalovirus m04 protein obtained from sparse NMR data reveals a conserved fold of the m02-m06 viral immune modulator family.
N.G.Sgourakis, K.Natarajan, J.Ying, B.Vogeli, L.F.Boyd, D.H.Margulies, A.Bax.
 
  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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