1u58
From Proteopedia
(New page: 200px<br /><applet load="1u58" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u58, resolution 1.90Å" /> '''Crystal structure of...) |
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| - | [[Image:1u58.gif|left|200px]]<br /><applet load="1u58" size=" | + | [[Image:1u58.gif|left|200px]]<br /><applet load="1u58" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u58, resolution 1.90Å" /> | caption="1u58, resolution 1.90Å" /> | ||
'''Crystal structure of the murine cytomegalovirus MHC-I homolog m144'''<br /> | '''Crystal structure of the murine cytomegalovirus MHC-I homolog m144'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Large DNA viruses of the herpesvirus family produce proteins that mimic | + | 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== | ==About this Structure== | ||
| - | 1U58 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Murid_herpesvirus_1 Murid herpesvirus 1] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1U58 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Murid_herpesvirus_1 Murid herpesvirus 1] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U58 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Guan, R.]] | [[Category: Guan, R.]] | ||
[[Category: Hicks, A.]] | [[Category: Hicks, A.]] | ||
| - | [[Category: Margulies, D | + | [[Category: Margulies, D H.]] |
[[Category: Natarajan, K.]] | [[Category: Natarajan, K.]] | ||
[[Category: Robinson, H.]] | [[Category: Robinson, H.]] | ||
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[[Category: mhc-i homolog]] | [[Category: mhc-i homolog]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:46 2008'' |
Revision as of 13:20, 21 February 2008
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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 Thu Feb 21 15:20:46 2008
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
