1inq
From Proteopedia
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|PDB= 1inq |SIZE=350|CAPTION= <scene name='initialview01'>1inq</scene>, resolution 2.20Å | |PDB= 1inq |SIZE=350|CAPTION= <scene name='initialview01'>1inq</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=DMS:DIMETHYL SULFOXIDE'>DMS</scene> | + | |LIGAND= <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= H2-Db ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= H2-Db ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1inq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1inq OCA], [http://www.ebi.ac.uk/pdbsum/1inq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1inq RCSB]</span> | ||
}} | }} | ||
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[[Category: Tilley, D.]] | [[Category: Tilley, D.]] | ||
[[Category: Villaflor, G.]] | [[Category: Villaflor, G.]] | ||
| - | [[Category: DMS]] | ||
[[Category: mhc complex]] | [[Category: mhc complex]] | ||
[[Category: minor histocompatibility antigen]] | [[Category: minor histocompatibility antigen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:22:12 2008'' |
Revision as of 18:22, 30 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | H2-Db (Mus musculus), B2M (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db
Overview
The mouse H13 minor histocompatibility (H) Ag, originally detected as a barrier to allograft transplants, is remarkable in that rejection is a consequence of an extremely subtle interchange, P4(Val/Ile), in a nonamer H2-D(b)-bound peptide. Moreover, H13 peptides lack the canonical P5(Asn) central anchor residue normally considered important for forming a peptide/MHC complex. To understand how these noncanonical peptide pMHC complexes form physiologically active TCR ligands, crystal structures of allelic H13 pD(b) complexes and a P5(Asn) anchored pD(b) analog were solved to high resolution. The structures show that the basis of TCRs to distinguish self from nonself H13 peptides is their ability to distinguish a single solvent-exposed methyl group. In addition, the structures demonstrate that there is no need for H13 peptides to derive any stabilization from interactions within the central C pocket to generate fully functional pMHC complexes. These results provide a structural explanation for a classical non-MHC-encoded H Ag, and they call into question the requirement for contact between anchor residues and the major MHC binding pockets in vaccine design.
About this Structure
1INQ is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
How H13 histocompatibility peptides differing by a single methyl group and lacking conventional MHC binding anchor motifs determine self-nonself discrimination., Ostrov DA, Roden MM, Shi W, Palmieri E, Christianson GJ, Mendoza L, Villaflor G, Tilley D, Shastri N, Grey H, Almo SC, Roopenian D, Nathenson SG, J Immunol. 2002 Jan 1;168(1):283-9. PMID:11751972
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