1inq: Difference between revisions

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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="450" color="white" frame="true" align="right" spinBox="true"
caption="1inq, resolution 2.20&Aring;" />
'''Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db'''<br />


==Overview==
==Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db==
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.
<StructureSection load='1inq' size='340' side='right'caption='[[1inq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/in/1inq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
 
*[[MHC 3D structures|MHC 3D structures]]
==Reference==
*[[MHC I 3D structures|MHC I 3D structures]]
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]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Almo SC]]
[[Category: Almo, S.C.]]
[[Category: Christianson GJ]]
[[Category: Christianson, G.J.]]
[[Category: Grey H]]
[[Category: Grey, H.]]
[[Category: Mendoza L]]
[[Category: Mendoza, L.]]
[[Category: Nathenson SG]]
[[Category: Nathenson, S.G.]]
[[Category: Ostrov DA]]
[[Category: Ostrov, D.A.]]
[[Category: Palmieri E]]
[[Category: Palmieri, E.]]
[[Category: Roden MM]]
[[Category: Roden, M.M.]]
[[Category: Roopenian D]]
[[Category: Roopenian, D.]]
[[Category: Shastri N]]
[[Category: Shastri, N.]]
[[Category: Shi W]]
[[Category: Shi, W.]]
[[Category: Tilley D]]
[[Category: Tilley, D.]]
[[Category: Villaflor G]]
[[Category: Villaflor, G.]]
[[Category: DMS]]
[[Category: mhc complex]]
[[Category: minor histocompatibility antigen]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:31:45 2007''

Latest revision as of 10:48, 3 April 2024

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

Structural highlights

1inq is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B2MG_MOUSE Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1inq, resolution 2.20Å

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