1u58: Difference between revisions

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[[Image:1u58.gif|left|200px]]<br /><applet load="1u58" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1u58.gif|left|200px]]<br /><applet load="1u58" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1u58, resolution 1.90Å" />

'''Crystal structure of the murine cytomegalovirus MHC-I homolog m144'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1U58 OCA].

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==

Line 16:

[[Category: Guan, R.]]

[[Category: Hicks, A.]]

[[Category: Margulies, D.H.]]

[[Category: Margulies, D H.]]

[[Category: Natarajan, K.]]

[[Category: Robinson, H.]]

Line 24:

[[Category: mhc-i homolog]]

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@@ Line 1: / Line 1: @@
-[[Image:1u58.gif|left|200px]]<br /><applet load="1u58" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1u58.gif|left|200px]]<br /><applet load="1u58" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1u58, resolution 1.90&Aring;" />
 '''Crystal structure of the murine cytomegalovirus MHC-I homolog m144'''<br />
 ==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.
+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==
-U58 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U58 OCA].
+U58 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==
@@ Line 16: / Line 16: @@
 [[Category: Guan, R.]]
 [[Category: Hicks, A.]]
-[[Category: Margulies, D.H.]]
+[[Category: Margulies, D H.]]
 [[Category: Natarajan, K.]]
 [[Category: Robinson, H.]]
@@ Line 24: / Line 24: @@
 [[Category: mhc-i homolog]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:51:01 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:46 2008''