1u58
From Proteopedia
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Crystal structure of the murine cytomegalovirus MHC-I homolog m144
Overview
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.
About this Structure
1U58 is a Single protein structure of sequence from Murid herpesvirus 1 and Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 03:51:01 2007
Categories: Murid herpesvirus 1 | Mus musculus | Single protein | Guan, R. | Hicks, A. | Margulies, D.H. | Natarajan, K. | Robinson, H. | Beta-2m | M144 | Mcmv | Mhc-i homolog
