1iao: Difference between revisions
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<StructureSection load='1iao' size='340' side='right'caption='[[1iao]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1iao' size='340' side='right'caption='[[1iao]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iao]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
<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> | |||
<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> | <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> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HA2D_MOUSE HA2D_MOUSE] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Peterson | [[Category: Peterson PA]] | ||
[[Category: Scott | [[Category: Scott CA]] | ||
[[Category: Teyton | [[Category: Teyton L]] | ||
[[Category: Wilson | [[Category: Wilson IA]] | ||
Latest revision as of 09:25, 9 August 2023
CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339CLASS II MHC I-AD IN COMPLEX WITH OVALBUMIN PEPTIDE 323-339
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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