4hs3: Difference between revisions
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==Crystal structure of H-2Kb with a disulfide stabilized F pocket in complex with the LCMV derived peptide GP34== | ==Crystal structure of H-2Kb with a disulfide stabilized F pocket in complex with the LCMV derived peptide GP34== | ||
<StructureSection load='4hs3' size='340' side='right' caption='[[4hs3]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4hs3' size='340' side='right'caption='[[4hs3]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hs3]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HS3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HS3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4hs3]] 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=4HS3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HS3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-K1, H2-K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), B2m ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4hs3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hs3 OCA], [http://pdbe.org/4hs3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hs3 RCSB], [http://www.ebi.ac.uk/pdbsum/4hs3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hs3 ProSAT]</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=4hs3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hs3 OCA], [http://pdbe.org/4hs3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hs3 RCSB], [http://www.ebi.ac.uk/pdbsum/4hs3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hs3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lk3 transgenic mice]] | |||
[[Category: Abualrous, E T]] | [[Category: Abualrous, E T]] | ||
[[Category: Achour, A]] | [[Category: Achour, A]] | ||
Revision as of 10:53, 27 March 2019
Crystal structure of H-2Kb with a disulfide stabilized F pocket in complex with the LCMV derived peptide GP34Crystal structure of H-2Kb with a disulfide stabilized F pocket in complex with the LCMV derived peptide GP34
Structural highlights
Function[HA1B_MOUSE] Involved in the presentation of foreign antigens to the immune system. [B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Publication Abstract from PubMedThe intracellular trafficking of major histocompatibility complex class I (MHC-I) proteins is directed by three quality control mechanisms that test for their structural integrity, which is correlated to the binding of high-affinity antigenic peptide ligands. To investigate which molecular features of MHC-I these quality control mechanisms detect, we have followed the hypothesis that suboptimally loaded MHC-I are characterized by their conformational mobility in the F pocket region of the peptide binding site. We have created a novel variant of an MHC-I protein, Kb-Y84C, in which two alpha helices in this region are linked by a disulfide bond that mimics the conformational and dynamic effects of bound high-affinity peptide. Kb-Y84C shows a remarkable increase in the binding affinity to its light chain, beta2m, and bypasses all three cellular quality control steps. Our data demonstrate that coupling between peptide and beta2m binding to the MHC-I heavy chain is mediated by conformational dynamics, that support of the folded conformation of MHC-I by beta2m plays a decisive role in passing the ER to cell surface transport quality controls, and that beta2m association is also tested by the cell surface quality control that leads to MHC-I endocytosis. Peptide-independent stabilization of MHC class I molecules breaches cellular quality control.,Hein Z, Uchtenhagen H, Abualrous ET, Saini SK, Janssen L, Van Hateren A, Wiek C, Hanenberg H, Momburg F, Achour A, Elliott T, Springer S, Boulanger D J Cell Sci. 2014 May 7. PMID:24806963[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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