2O5N
Crystal structure of a Viral Glycoprotein
Summary for 2O5N
| Entry DOI | 10.2210/pdb2o5n/pdb |
| Descriptor | MuHV1gpm153, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | m153, mouse cytomegalovirus, mhc-i-like, m145 family, mhc-iv, ig-superfamily, alpha-beta protein, viral protein |
| Biological source | Murid herpesvirus 1 (Murine cytomegalovirus) |
| Total number of polymer chains | 2 |
| Total formula weight | 74408.24 |
| Authors | Mans, J.,Natarajan, K.,Robinson, H.,Margulies, D.H. (deposition date: 2006-12-06, release date: 2007-09-25, Last modification date: 2024-10-16) |
| Primary citation | Mans, J.,Natarajan, K.,Balbo, A.,Schuck, P.,Eikel, D.,Hess, S.,Robinson, H.,Simic, H.,Jonjic, S.,Tiemessen, C.T.,Margulies, D.H. Cellular Expression and Crystal Structure of the Murine Cytomegalovirus Major Histocompatibility Complex Class I-like Glycoprotein, m153. J.Biol.Chem., 282:35247-35258, 2007 Cited by PubMed Abstract: Mouse cytomegalovirus (MCMV), a beta-herpesvirus that establishes latent and persistent infections in mice, is a valuable model for studying complex virus-host interactions. MCMV encodes the m145 family of putative immunoevasins with predicted major histocompatibility complex, class I (MHC-I) structure. Functions attributed to some family members include down-regulation of host MHC-I (m152) and NKG2D ligands (m145, m152, and m155) and interaction with inhibitory or activating NK receptors (m157). We present the cellular, biochemical, and structural characterization of m153, which is a heavily glycosylated homodimer, that does not require beta2m or peptide and is expressed at the surface of MCMV-infected cells. Its 2.4-A crystal structure confirms that this compact molecule preserves an MHC-I-like fold and reveals a novel mode of dimerization, confirmed by site-directed mutagenesis, and a distinctive disulfide-stabilized extended N terminus. The structure provides a useful framework for comparative analysis of the divergent members of the m145 family. PubMed: 17897947DOI: 10.1074/jbc.M706782200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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