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''' | + | {{Structure |
| + | |PDB= 1f3j |SIZE=350|CAPTION= <scene name='initialview01'>1f3j</scene>, resolution 3.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HISTOCOMPATIBILITY ANTIGEN I-AG7''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F3J is a [ | + | 1F3J is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3J OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10894169 10894169] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: peptide complex]] | [[Category: peptide complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:54 2008'' |
Revision as of 09:03, 20 March 2008
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| , resolution 3.1Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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