View source for 4hs3


==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]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hs3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mammarenavirus_choriomeningitidis Mammarenavirus choriomeningitidis] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4HS3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4hs3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hs3 OCA], [https://pdbe.org/4hs3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hs3 RCSB], [https://www.ebi.ac.uk/pdbsum/4hs3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hs3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA1B_MOUSE HA1B_MOUSE] Involved in the presentation of foreign antigens to the immune system.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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<ref>PMID:24806963</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hs3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mammarenavirus choriomeningitidis]]
[[Category: Mus musculus]]
[[Category: Abualrous ET]]
[[Category: Achour A]]
[[Category: Boulanger B]]
[[Category: Elliott T]]
[[Category: Hein Z]]
[[Category: Springer S]]
[[Category: Uchtenhagen H]]
[[Category: Werner J]]
[[Category: Zacharias M]]