1juf

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[[Image:1juf.jpg|left|200px]]<br /><applet load="1juf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1juf.jpg|left|200px]]
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caption="1juf, resolution 2.00&Aring;" />
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'''Structure of Minor Histocompatibility Antigen peptide, H13b, complexed to H2-Db'''<br />
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{{Structure
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|PDB= 1juf |SIZE=350|CAPTION= <scene name='initialview01'>1juf</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= H2-D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), beta-2-microglobulin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), H13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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'''Structure of Minor Histocompatibility Antigen peptide, H13b, complexed to H2-Db'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1JUF 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=1JUF OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11751972 11751972]
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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]]
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[[Category: h2-db]]
[[Category: h2-db]]
[[Category: mhc class-i]]
[[Category: mhc class-i]]
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[[Category: minor histocompatibility antigens]]
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[[Category: minor histocompatibility antigen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:08:37 2008''

Revision as of 10:08, 20 March 2008


PDB ID 1juf

Drag the structure with the mouse to rotate
, resolution 2.00Å
Gene: H2-D (Mus musculus), beta-2-microglobulin (Mus musculus), H13 (Mus musculus)
Coordinates: save as pdb, mmCIF, xml



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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