1f3j: Difference between revisions

New page: left|200px<br /><applet load="1f3j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f3j, resolution 3.1Å" /> '''HISTOCOMPATIBILITY AN...
 
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[[Image:1f3j.jpg|left|200px]]<br /><applet load="1f3j" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1f3j.jpg|left|200px]]<br /><applet load="1f3j" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1f3j, resolution 3.1&Aring;" />
caption="1f3j, resolution 3.1&Aring;" />
'''HISTOCOMPATIBILITY ANTIGEN I-AG7'''<br />
'''HISTOCOMPATIBILITY ANTIGEN I-AG7'''<br />


==Overview==
==Overview==
We have determined the crystal structure of I-Ag7, an integral component, in murine type I diabetes development. Several features distinguish I-Ag7, from other non-autoimmune-associated MHC class II molecules, including, novel peptide and heterodimer pairing interactions. The binding groove of, I-Ag7 is unusual at both terminal ends, with a potentially solvent-exposed, channel at the base of the P1 pocket and a widened entrance to the P9, pocket. Peptide binding studies with variants of the hen egg lysozyme, I-Ag7 epitope HEL(11-25) support a comprehensive structure-based I-Ag7, binding motif. Residues critical for T cell recognition were investigated, with a panel of HEL(11-25)-restricted clones, which uncovered P1, anchor-dependent structural variations. These results establish a, framework for future experiments directed at understanding the role of, I-Ag7 in autoimmunity.
We have determined the crystal structure of I-Ag7, an integral component in murine type I diabetes development. Several features distinguish I-Ag7 from other non-autoimmune-associated MHC class II molecules, including novel peptide and heterodimer pairing interactions. The binding groove of I-Ag7 is unusual at both terminal ends, with a potentially solvent-exposed channel at the base of the P1 pocket and a widened entrance to the P9 pocket. Peptide binding studies with variants of the hen egg lysozyme I-Ag7 epitope HEL(11-25) support a comprehensive structure-based I-Ag7 binding motif. Residues critical for T cell recognition were investigated with a panel of HEL(11-25)-restricted clones, which uncovered P1 anchor-dependent structural variations. These results establish a framework for future experiments directed at understanding the role of I-Ag7 in autoimmunity.


==About this Structure==
==About this Structure==
1F3J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F3J OCA].  
1F3J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3J OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Fremont, D.H.]]
[[Category: Fremont, D H.]]
[[Category: Latek, R.R.]]
[[Category: Latek, R R.]]
[[Category: Unanue, E.R.]]
[[Category: Unanue, E R.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: histocompatibility antigen]]
[[Category: histocompatibility antigen]]
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[[Category: peptide complex]]
[[Category: peptide complex]]


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