1iak

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(New page: 200px<br /><applet load="1iak" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iak, resolution 1.9&Aring;" /> '''HISTOCOMPATIBILITY AN...)
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[[Image:1iak.gif|left|200px]]<br /><applet load="1iak" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1iak, resolution 1.9&Aring;" />
 
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'''HISTOCOMPATIBILITY ANTIGEN I-AK'''<br />
 
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==Overview==
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==HISTOCOMPATIBILITY ANTIGEN I-AK==
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We have determined the structure of murine MHC class II I-Ak in complex, with a naturally processed peptide from hen egg lysozyme (HEL residues, 50-62) at 1.9 A resolution. These results provide a structural basis for, the I-Ak peptide-binding motif. Binding is established by the deep burial, of five anchor side chains into specific pockets of the I-Ak binding, groove, with a zen-like fit of an aspartic acid in the P1 pocket. We also, show that in the I-Ak alpha chain, a bulge occurs in the first strand of, the peptide-binding platform, an insertion probably common to all I-A and, HLA-DQ alleles. The I-Ak beta chain has a deletion in the helical region, adjacent to the P7 pocket and an insertion in the helical region, neighboring the P1 pocket. As a result of these structural features, the, extended HEL peptide dips low into the center of the I-Ak groove and, reaches toward solvent at its C-terminal end.
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<StructureSection load='1iak' size='340' side='right'caption='[[1iak]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1iak]] 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=1IAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAK 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]] 1.9&#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=1iak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iak OCA], [https://pdbe.org/1iak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iak RCSB], [https://www.ebi.ac.uk/pdbsum/1iak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iak ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HA2K_MOUSE HA2K_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/1iak_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1iak 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 structure of murine MHC class II I-Ak in complex with a naturally processed peptide from hen egg lysozyme (HEL residues 50-62) at 1.9 A resolution. These results provide a structural basis for the I-Ak peptide-binding motif. Binding is established by the deep burial of five anchor side chains into specific pockets of the I-Ak binding groove, with a zen-like fit of an aspartic acid in the P1 pocket. We also show that in the I-Ak alpha chain, a bulge occurs in the first strand of the peptide-binding platform, an insertion probably common to all I-A and HLA-DQ alleles. The I-Ak beta chain has a deletion in the helical region adjacent to the P7 pocket and an insertion in the helical region neighboring the P1 pocket. As a result of these structural features, the extended HEL peptide dips low into the center of the I-Ak groove and reaches toward solvent at its C-terminal end.
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==About this Structure==
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Crystal structure of I-Ak in complex with a dominant epitope of lysozyme.,Fremont DH, Monnaie D, Nelson CA, Hendrickson WA, Unanue ER Immunity. 1998 Mar;8(3):305-17. PMID:9529148<ref>PMID:9529148</ref>
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1IAK 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=1IAK 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 structure of I-Ak in complex with a dominant epitope of lysozyme., Fremont DH, Monnaie D, Nelson CA, Hendrickson WA, Unanue ER, Immunity. 1998 Mar;8(3):305-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9529148 9529148]
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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 1iak" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Fremont, D.H.]]
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[[Category: Hendrickson, W.A.]]
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[[Category: Unanue, E.R.]]
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[[Category: NAG]]
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[[Category: histocompatibility antigen]]
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[[Category: mhc]]
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[[Category: peptide complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:13:16 2007''
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==See Also==
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*[[MHC 3D structures|MHC 3D structures]]
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*[[MHC II 3D structures|MHC II 3D structures]]
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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]]
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[[Category: Mus musculus]]
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[[Category: Fremont DH]]
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[[Category: Hendrickson WA]]
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[[Category: Unanue ER]]

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HISTOCOMPATIBILITY ANTIGEN I-AK

PDB ID 1iak

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