1inq: Difference between revisions
New page: left|200px<br /><applet load="1inq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1inq, resolution 2.20Å" /> '''Structure of Minor H... |
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[[Image:1inq.jpg|left|200px]]<br /><applet load="1inq" size=" | [[Image:1inq.jpg|left|200px]]<br /><applet load="1inq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1inq, resolution 2.20Å" /> | caption="1inq, resolution 2.20Å" /> | ||
'''Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db'''<br /> | '''Structure of Minor Histocompatibility Antigen peptide, H13a, 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== | ||
1INQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with DMS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1INQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=DMS:'>DMS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INQ 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.]] | ||
[[Category: Shastri, N.]] | [[Category: Shastri, N.]] | ||
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[[Category: minor histocompatibility antigen]] | [[Category: minor histocompatibility antigen]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:41 2008'' | ||
Revision as of 14:13, 21 February 2008
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Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db
OverviewOverview
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 StructureAbout this Structure
1INQ is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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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