1juf
From Proteopedia
(New page: 200px<br /><applet load="1juf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1juf, resolution 2.00Å" /> '''Structure of Minor H...) |
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| - | [[Image:1juf.jpg|left|200px]]<br /><applet load="1juf" size=" | + | [[Image:1juf.jpg|left|200px]]<br /><applet load="1juf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1juf, resolution 2.00Å" /> | caption="1juf, resolution 2.00Å" /> | ||
'''Structure of Minor Histocompatibility Antigen peptide, H13b, complexed to H2-Db'''<br /> | '''Structure of Minor Histocompatibility Antigen peptide, H13b, complexed to H2-Db'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The mouse H13 minor histocompatibility (H) Ag, originally detected as a | + | 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== | ==About this Structure== | ||
| - | 1JUF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1JUF is a [http://en.wikipedia.org/wiki/Protein_complex 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=1JUF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Almo, S | + | [[Category: Almo, S C.]] |
| - | [[Category: Christianson, G | + | [[Category: Christianson, G J.]] |
[[Category: Grey, H.]] | [[Category: Grey, H.]] | ||
[[Category: Mendoza, L.]] | [[Category: Mendoza, L.]] | ||
| - | [[Category: Nathenson, S | + | [[Category: Nathenson, S G.]] |
| - | [[Category: Ostrov, D | + | [[Category: Ostrov, D A.]] |
[[Category: Palmieri, E.]] | [[Category: Palmieri, E.]] | ||
| - | [[Category: Roden, M | + | [[Category: Roden, M M.]] |
| - | [[Category: Roopenian, D | + | [[Category: Roopenian, D C.]] |
[[Category: Shastri, N.]] | [[Category: Shastri, N.]] | ||
[[Category: Shi, W.]] | [[Category: Shi, W.]] | ||
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[[Category: minor histocompatibility antigens]] | [[Category: minor histocompatibility antigens]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:53 2008'' |
Revision as of 11:26, 21 February 2008
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Structure of Minor Histocompatibility Antigen peptide, H13b, 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
1JUF 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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