1f3j: Difference between revisions

Revision as of 02:37, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1f3j.png

Template:STRUCTURE 1f3j

HISTOCOMPATIBILITY ANTIGEN I-AG7HISTOCOMPATIBILITY ANTIGEN I-AG7

Template:ABSTRACT PUBMED 10894169

About this StructureAbout this Structure

1F3J is a Protein complex structure of sequences from Gallus gallus and Mus musculus. 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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OCA

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-==Overview==
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-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.
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 [[Category: Mhc]]
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