1inq
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1inq.jpg|left|200px]] | + | [[Image:1inq.jpg|left|200px]] |
| - | + | ||
| - | '''Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db''' | + | {{Structure |
| + | |PDB= 1inq |SIZE=350|CAPTION= <scene name='initialview01'>1inq</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=DMS:DIMETHYL SULFOXIDE'>DMS</scene> | ||
| + | |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]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1INQ is a [ | + | 1INQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INQ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11751972 11751972] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 30: | Line 39: | ||
[[Category: minor histocompatibility antigen]] | [[Category: minor histocompatibility antigen]] | ||
| - | ''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 11:52:37 2008'' |
Revision as of 09:52, 20 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | H2-Db (Mus musculus), B2M (Mus musculus) | ||||||
| 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
Page seeded by OCA on Thu Mar 20 11:52:37 2008
