6tdr: Difference between revisions
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<StructureSection load='6tdr' size='340' side='right'caption='[[6tdr]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='6tdr' size='340' side='right'caption='[[6tdr]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6tdr]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TDR OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6tdr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TDR FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.75Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6tdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tdr OCA], [https://pdbe.org/6tdr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tdr RCSB], [https://www.ebi.ac.uk/pdbsum/6tdr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tdr ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/F6IQS1_HUMAN F6IQS1_HUMAN] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6tdr" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6tdr" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
*[[MHC 3D structures|MHC 3D structures]] | |||
*[[MHC I 3D structures|MHC I 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Anjanappa R]] | ||
[[Category: | [[Category: Garcia Alai M]] | ||
[[Category: Meijers | [[Category: Meijers R]] | ||
[[Category: Springer | [[Category: Springer S]] | ||
Latest revision as of 16:00, 24 January 2024
Crystal structure of the disulfide engineered HLA-A0201 molecule devoid of peptide (annealed)Crystal structure of the disulfide engineered HLA-A0201 molecule devoid of peptide (annealed)
Structural highlights
FunctionPublication Abstract from PubMedMajor Histocompatibility Complex (MHC) class I molecules selectively bind peptides for presentation to cytotoxic T cells. The peptide-free state of these molecules is not well understood. Here, we characterize a disulfide-stabilized version of the human class I molecule HLA-A*02:01 that is stable in the absence of peptide and can readily exchange cognate peptides. We present X-ray crystal structures of the peptide-free state of HLA-A*02:01, together with structures that have dipeptides bound in the A and F pockets. These structural snapshots reveal that the amino acid side chains lining the binding pockets switch in a coordinated fashion between a peptide-free unlocked state and a peptide-bound locked state. Molecular dynamics simulations suggest that the opening and closing of the F pocket affects peptide ligand conformations in adjacent binding pockets. We propose that peptide binding is co-determined by synergy between the binding pockets of the MHC molecule. Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection.,Anjanappa R, Garcia-Alai M, Kopicki JD, Lockhauserbaumer J, Aboelmagd M, Hinrichs J, Nemtanu IM, Uetrecht C, Zacharias M, Springer S, Meijers R Nat Commun. 2020 Mar 11;11(1):1314. doi: 10.1038/s41467-020-14862-4. PMID:32161266[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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