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New page: left|200px<br /><applet load="1es0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1es0, resolution 2.60Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1es0.gif|left|200px]]<br /><applet load="1es0" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1es0.gif|left|200px]]<br /><applet load="1es0" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1es0, resolution 2.60&Aring;" />
caption="1es0, resolution 2.60&Aring;" />
'''CRYSTAL STRUCTURE OF THE MURINE CLASS II ALLELE I-A(G7) COMPLEXED WITH THE GLUTAMIC ACID DECARBOXYLASE (GAD65) PEPTIDE 207-220'''<br />
'''CRYSTAL STRUCTURE OF THE MURINE CLASS II ALLELE I-A(G7) COMPLEXED WITH THE GLUTAMIC ACID DECARBOXYLASE (GAD65) PEPTIDE 207-220'''<br />


==Overview==
==Overview==
Susceptibility to murine and human insulin-dependent diabetes mellitus, correlates strongly with major histocompatibility complex (MHC) class II, I-A or HLA-DQ alleles that lack an aspartic acid at position beta57. I-Ag7, lacks this aspartate and is the only class II allele expressed by the, nonobese diabetic mouse. The crystal structure of I-Ag7 was determined at, 2.6 angstrom resolution as a complex with a high-affinity peptide from the, autoantigen glutamic acid decarboxylase (GAD) 65. I-Ag7 has a, substantially wider peptide-binding groove around beta57, which accounts, for distinct peptide preferences compared with other MHC class II alleles., Loss of Asp(beta57) leads to an oxyanion hole in I-Ag7 that can be filled, by peptide carboxyl residues or, perhaps, through interaction with the T, cell receptor.
Susceptibility to murine and human insulin-dependent diabetes mellitus correlates strongly with major histocompatibility complex (MHC) class II I-A or HLA-DQ alleles that lack an aspartic acid at position beta57. I-Ag7 lacks this aspartate and is the only class II allele expressed by the nonobese diabetic mouse. The crystal structure of I-Ag7 was determined at 2.6 angstrom resolution as a complex with a high-affinity peptide from the autoantigen glutamic acid decarboxylase (GAD) 65. I-Ag7 has a substantially wider peptide-binding groove around beta57, which accounts for distinct peptide preferences compared with other MHC class II alleles. Loss of Asp(beta57) leads to an oxyanion hole in I-Ag7 that can be filled by peptide carboxyl residues or, perhaps, through interaction with the T cell receptor.


==About this Structure==
==About this Structure==
1ES0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1ES0 OCA].  
1ES0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1ES0 OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Corper, A.L.]]
[[Category: Corper, A L.]]
[[Category: Teyton, L.]]
[[Category: Teyton, L.]]
[[Category: Wilson, I.A.]]
[[Category: Wilson, I A.]]
[[Category: class ii mhc i-a(g7)]]
[[Category: class ii mhc i-a(g7)]]
[[Category: histocompatibility antigen]]
[[Category: histocompatibility antigen]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:15:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:53 2008''