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1f3j
From Proteopedia
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[[Image:1f3j.jpg|left|200px]] | [[Image:1f3j.jpg|left|200px]] | ||
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'''HISTOCOMPATIBILITY ANTIGEN I-AG7''' | '''HISTOCOMPATIBILITY ANTIGEN I-AG7''' | ||
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[[Category: Latek, R R.]] | [[Category: Latek, R R.]] | ||
[[Category: Unanue, E R.]] | [[Category: Unanue, E R.]] | ||
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| - | [[Category: | + | [[Category: Mhc]] |
| - | [[Category: | + | [[Category: Peptide complex]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:51:05 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:51, 2 May 2008
HISTOCOMPATIBILITY ANTIGEN I-AG7
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.
About this Structure
1F3J is a Protein complex structure of sequences from Gallus gallus and Mus musculus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 15:51:05 2008
