1iak: Difference between revisions
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<StructureSection load='1iak' size='340' side='right' caption='[[1iak]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1iak' size='340' side='right' caption='[[1iak]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1iak]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1iak]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IAK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iak OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iak RCSB], [http://www.ebi.ac.uk/pdbsum/1iak PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iak OCA], [http://pdbe.org/1iak PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iak RCSB], [http://www.ebi.ac.uk/pdbsum/1iak PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1iak" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Major histocompatibility complex|Major histocompatibility complex]] | *[[Major histocompatibility complex|Major histocompatibility complex]] | ||
*[[NADP-dependent malic enzyme|NADP-dependent malic enzyme]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Lk3 transgenic mice]] | ||
[[Category: Fremont, D H]] | [[Category: Fremont, D H]] | ||
[[Category: Hendrickson, W A]] | [[Category: Hendrickson, W A]] | ||
Revision as of 08:53, 10 September 2015
HISTOCOMPATIBILITY ANTIGEN I-AKHISTOCOMPATIBILITY ANTIGEN I-AK
Structural highlights
Function[LYSC_LOPLE] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Evolutionary 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 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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