1inq

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(New page: 200px<br /><applet load="1inq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1inq, resolution 2.20&Aring;" /> '''Structure of Minor H...)
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[[Image:1inq.jpg|left|200px]]<br /><applet load="1inq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1inq, resolution 2.20&Aring;" />
 
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'''Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db'''<br />
 
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==Overview==
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==Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db==
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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.
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<StructureSection load='1inq' size='340' side='right'caption='[[1inq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1inq]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1INQ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1inq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1inq OCA], [https://pdbe.org/1inq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1inq RCSB], [https://www.ebi.ac.uk/pdbsum/1inq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1inq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B2MG_MOUSE B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/in/1inq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1inq ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1INQ OCA].
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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*[[MHC 3D structures|MHC 3D structures]]
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==Reference==
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*[[MHC I 3D structures|MHC I 3D structures]]
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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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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Almo SC]]
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[[Category: Almo, S.C.]]
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[[Category: Christianson GJ]]
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[[Category: Christianson, G.J.]]
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[[Category: Grey H]]
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[[Category: Grey, H.]]
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[[Category: Mendoza L]]
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[[Category: Mendoza, L.]]
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[[Category: Nathenson SG]]
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[[Category: Nathenson, S.G.]]
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[[Category: Ostrov DA]]
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[[Category: Ostrov, D.A.]]
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[[Category: Palmieri E]]
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[[Category: Palmieri, E.]]
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[[Category: Roden MM]]
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[[Category: Roden, M.M.]]
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[[Category: Roopenian D]]
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[[Category: Roopenian, D.]]
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[[Category: Shastri N]]
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[[Category: Shastri, N.]]
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[[Category: Shi W]]
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[[Category: Shi, W.]]
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[[Category: Tilley D]]
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[[Category: Tilley, D.]]
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[[Category: Villaflor G]]
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[[Category: Villaflor, G.]]
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[[Category: DMS]]
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[[Category: mhc complex]]
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[[Category: minor histocompatibility antigen]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:31:45 2007''
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Current revision

Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db

PDB ID 1inq

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