1inq
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1inq.jpg|left|200px]] | [[Image:1inq.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1inq", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1inq| PDB=1inq | SCENE= }} | |
| - | | | + | |
| - | | | + | |
| - | }} | + | |
'''Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db''' | '''Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db''' | ||
| Line 38: | Line 35: | ||
[[Category: Tilley, D.]] | [[Category: Tilley, D.]] | ||
[[Category: Villaflor, G.]] | [[Category: Villaflor, G.]] | ||
| - | [[Category: | + | [[Category: Mhc complex]] |
| - | [[Category: | + | [[Category: Minor histocompatibility antigen]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:11:50 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:11, 2 May 2008
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 Fri May 2 20:11:50 2008
