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| [[Image:1f3j.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1f3j| PDB=1f3j | SCENE= }} | | {{STRUCTURE_1f3j| PDB=1f3j | SCENE= }} |
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| '''HISTOCOMPATIBILITY ANTIGEN I-AG7'''
| | ===HISTOCOMPATIBILITY ANTIGEN I-AG7=== |
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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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10894169}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10894169 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10894169}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mhc]] | | [[Category: Mhc]] |
| [[Category: Peptide complex]] | | [[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 Tue Jul 1 02:37:00 2008'' |