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=" | [[Image:1f3j.jpg|left|200px]]<br /><applet load="1f3j" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1f3j, resolution 3.1Å" /> | caption="1f3j, resolution 3.1Å" /> | ||
'''HISTOCOMPATIBILITY ANTIGEN I-AG7'''<br /> | '''HISTOCOMPATIBILITY ANTIGEN I-AG7'''<br /> | ||
==Overview== | ==Overview== | ||
We have determined the crystal structure of I-Ag7, an integral component | 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:// | 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 | [[Category: Fremont, D H.]] | ||
[[Category: Latek, R | [[Category: Latek, R R.]] | ||
[[Category: Unanue, E | [[Category: Unanue, E R.]] | ||
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: histocompatibility antigen]] | [[Category: histocompatibility antigen]] | ||
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[[Category: peptide complex]] | [[Category: peptide complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:25 2008'' | ||
Revision as of 13:34, 21 February 2008
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HISTOCOMPATIBILITY ANTIGEN I-AG7
OverviewOverview
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 StructureAbout this Structure
1F3J is a Protein complex structure of sequences from Gallus gallus and Mus musculus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of peptide binding and presentation by the type I diabetes-associated MHC class II molecule of NOD mice., Latek RR, Suri A, Petzold SJ, Nelson CA, Kanagawa O, Unanue ER, Fremont DH, Immunity. 2000 Jun;12(6):699-710. PMID:10894169
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