1u58

Publication Abstract from PubMed

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.

Crystal structure of the murine cytomegalovirus MHC-I homolog m144.,Natarajan K, Hicks A, Mans J, Robinson H, Guan R, Mariuzza RA, Margulies DH J Mol Biol. 2006 Apr 21;358(1):157-71. Epub 2006 Feb 9. PMID:16500675^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.