2iad: Difference between revisions

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New page: left|200px<br /><applet load="2iad" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iad, resolution 2.4Å" /> '''CLASS II MHC I-AD IN ...
 
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[[Image:2iad.gif|left|200px]]<br /><applet load="2iad" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2iad, resolution 2.4&Aring;" />
'''CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138'''<br />


==Overview==
==CLASS II MHC I-AD IN COMPLEX WITH AN INFLUENZA HEMAGGLUTININ PEPTIDE 126-138==
We have determined the structures of I-Ad covalently linked to an, ovalbumin peptide (OVA323-339) and to an influenza virus hemagglutinin, peptide (HA126-138). The floor of the peptide-binding groove contains an, unusual beta bulge, not seen in I-E and DR structures, that affects, numerous interactions between the alpha and beta chains and bound peptide., Unlike other MHC-peptide complexes, the peptides do not insert any large, anchor residues into the binding pockets of the shallow I-Ad binding, groove. The previously identified six-residue "core" binding motif of I-Ad, occupies only the P4 to P9 pockets, implying that specificity of T cell, receptor recognition of I-Ad-peptide complexes can be accomplished by, peptides that only partially fill the MHC groove.
<StructureSection load='2iad' size='340' side='right'caption='[[2iad]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2iad]] is a 2 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=2IAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IAD 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]] 2.4&#8491;</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=2iad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iad OCA], [https://pdbe.org/2iad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iad RCSB], [https://www.ebi.ac.uk/pdbsum/2iad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iad ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA2D_MOUSE HA2D_MOUSE]
== 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/ia/2iad_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2iad ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have determined the structures of I-Ad covalently linked to an ovalbumin peptide (OVA323-339) and to an influenza virus hemagglutinin peptide (HA126-138). The floor of the peptide-binding groove contains an unusual beta bulge, not seen in I-E and DR structures, that affects numerous interactions between the alpha and beta chains and bound peptide. Unlike other MHC-peptide complexes, the peptides do not insert any large anchor residues into the binding pockets of the shallow I-Ad binding groove. The previously identified six-residue "core" binding motif of I-Ad occupies only the P4 to P9 pockets, implying that specificity of T cell receptor recognition of I-Ad-peptide complexes can be accomplished by peptides that only partially fill the MHC groove.


==About this Structure==
Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues.,Scott CA, Peterson PA, Teyton L, Wilson IA Immunity. 1998 Mar;8(3):319-29. PMID:9529149<ref>PMID:9529149</ref>
2IAD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IAD OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues., Scott CA, Peterson PA, Teyton L, Wilson IA, Immunity. 1998 Mar;8(3):319-29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9529149 9529149]
</div>
<div class="pdbe-citations 2iad" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Peterson PA]]
[[Category: Peterson, P.A.]]
[[Category: Scott CA]]
[[Category: Scott, C.A.]]
[[Category: Teyton L]]
[[Category: Teyton, L.]]
[[Category: Wilson IA]]
[[Category: Wilson, I.A.]]
[[Category: class ii mhc i-ad]]
[[Category: mhc ii]]
 
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Retrieved from "https://proteopedia.org/2iad"