1U58
Crystal structure of the murine cytomegalovirus MHC-I homolog m144
Summary for 1U58
| Entry DOI | 10.2210/pdb1u58/pdb |
| Descriptor | MHC-I homolog m144, beta-2-microglobulin (3 entities in total) |
| Functional Keywords | mcmv, mhc-i homolog, m144, beta-2m, immune system |
| Biological source | Murid herpesvirus 1 (Murine cytomegalovirus) More |
| Total number of polymer chains | 2 |
| Total formula weight | 40011.81 |
| Authors | Natarajan, K.,Hicks, A.,Robinson, H.,Guan, R.,Margulies, D.H. (deposition date: 2004-07-27, release date: 2005-07-19, Last modification date: 2024-11-13) |
| Primary citation | Natarajan, K.,Hicks, A.,Mans, J.,Robinson, H.,Guan, R.,Mariuzza, R.A.,Margulies, D.H. Crystal structure of the murine cytomegalovirus MHC-I homolog m144. J.Mol.Biol., 358:157-171, 2006 Cited by PubMed Abstract: Large DNA viruses of the herpesvirus family produce proteins that mimic host MHC-I molecules as part of their immunoevasive strategy. The m144 glycoprotein, expressed by murine cytomegalovirus, is thought to be an MHC-I homolog whose expression prolongs viral survival in vivo by preventing natural killer cell activation. To explore the structural basis of this m144 function, we have determined the three-dimensional structure of an m144/beta2-microglobulin (beta2m) complex at 1.9A resolution. This structure reveals the canonical features of MHC-I molecules including readily identifiable alpha1, alpha2, and alpha3 domains. A unique disulfide bond links the alpha1 helix to the beta-sheet floor, explaining the known thermal stability of m144. Close juxtaposition of the alpha1 and alpha2 helices and the lack of critical residues that normally contribute to anchoring the peptide N and C termini eliminates peptide binding. A region of 13 amino acid residues, corresponding to the amino-terminal portion of the alpha2 helix, is missing in the electron density map, suggesting an area of structural flexibility that may be involved in ligand binding. PubMed: 16500675DOI: 10.1016/j.jmb.2006.01.068 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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