1iao: Difference between revisions

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[[Image:1iao.gif|left|200px]]


{{Structure
==CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339==
|PDB= 1iao |SIZE=350|CAPTION= <scene name='initialview01'>1iao</scene>, resolution 2.6&Aring;
<StructureSection load='1iao' size='340' side='right'caption='[[1iao]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
<table><tr><td colspan='2'>[[1iao]] 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=1IAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAO FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iao OCA], [https://pdbe.org/1iao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iao RCSB], [https://www.ebi.ac.uk/pdbsum/1iao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iao ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iao OCA], [http://www.ebi.ac.uk/pdbsum/1iao PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iao RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/HA2D_MOUSE HA2D_MOUSE]
 
== Evolutionary Conservation ==
'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ia/1iao_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=1iao 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.
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>
1IAO 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=1IAO 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://www.ncbi.nlm.nih.gov/pubmed/9529149 9529149]
</div>
<div class="pdbe-citations 1iao" 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]]
[[Category: i-a]]
[[Category: mhc ii]]
[[Category: ovalbumin peptide]]
 
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