View source for 5wer


==Crystal Structure of TAPBPR and H2-Dd complex==
<StructureSection load='5wer' size='340' side='right'caption='[[5wer]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wer]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=5WER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WER 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]] 3.412&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5wer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wer OCA], [https://pdbe.org/5wer PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wer RCSB], [https://www.ebi.ac.uk/pdbsum/5wer PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wer ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA12_MOUSE HA12_MOUSE] Involved in the presentation of foreign antigens to the immune system.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Central to CD8+ T-cell mediated immunity is the recognition of peptide-major histocompatibility complex class I (pMHC-I) proteins displayed by antigen-presenting cells. Chaperone-mediated loading of high-affinity peptides onto MHC-I is a key step in the MHC-I antigen presentation pathway. However, the structure of MHC-I with a chaperone that facilitates peptide loading has not been determined. We report the crystal structure of MHC-I in complex with the peptide editor TAPBPR (TAP binding protein, related), a tapasin homolog. TAPBPR remodels the peptide-binding groove of MHC-I, resulting in the release of low-affinity peptide. Changes include groove relaxation, modifications of key binding pockets, and domain adjustments. This structure captures a peptide-receptive state of MHC-I and provides insights into the mechanism of peptide editing by TAPBPR and, by analogy, tapasin.

Crystal structure of a TAPBPR-MHC-I complex reveals the mechanism of peptide editing in antigen presentation.,Jiang J, Natarajan K, Boyd LF, Morozov GI, Mage MG, Margulies DH Science. 2017 Oct 12. pii: eaao5154. doi: 10.1126/science.aao5154. PMID:29025991<ref>PMID:29025991</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wer" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Boyd LF]]
[[Category: Jiang JS]]
[[Category: Margulies DH]]
[[Category: Natarajan K]]