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1iao

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(New page: 200px<br /><applet load="1iao" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iao, resolution 2.6&Aring;" /> '''CLASS II MHC I-AD IN ...)
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[[Image:1iao.gif|left|200px]]<br /><applet load="1iao" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1iao, resolution 2.6&Aring;" />
 
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'''CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339'''<br />
 
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==Overview==
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==CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339==
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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.
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<StructureSection load='1iao' size='340' side='right'caption='[[1iao]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 2.6&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HA2D_MOUSE HA2D_MOUSE]
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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/ia/1iao_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=1iao ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1IAO 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 NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IAO OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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<div class="pdbe-citations 1iao" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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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: Peterson PA]]
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[[Category: Peterson, P.A.]]
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[[Category: Scott CA]]
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[[Category: Scott, C.A.]]
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[[Category: Teyton L]]
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[[Category: Teyton, L.]]
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[[Category: Wilson IA]]
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[[Category: Wilson, I.A.]]
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[[Category: NAG]]
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[[Category: class ii mhc]]
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[[Category: i-a]]
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[[Category: mhc ii]]
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[[Category: ovalbumin peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:13:21 2007''
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Current revision

CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339

PDB ID 1iao

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