6b9k: Difference between revisions

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'''Unreleased structure'''


The entry 6b9k is ON HOLD  until Paper Publication
==Solution NMR Structure of Unbound P18-I10==
<StructureSection load='6b9k' size='340' side='right' caption='[[6b9k]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6b9k]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B9K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B9K FirstGlance]. <br>
</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=6b9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b9k OCA], [http://pdbe.org/6b9k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b9k RCSB], [http://www.ebi.ac.uk/pdbsum/6b9k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b9k ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chaperones TAPBPR and tapasin associate with class I major histocompatibility complexes (MHC-I) to promote optimization (editing) of peptide cargo. Here, we use solution NMR to investigate the mechanism of peptide exchange. We identify TAPBPR-induced conformational changes on conserved MHC-I molecular surfaces, consistent with our independently determined X-ray structure of the complex. Dynamics present in the empty MHC-I are stabilized by TAPBPR and become progressively dampened with increasing peptide occupancy. Incoming peptides are recognized according to the global stability of the final pMHC-I product and anneal in a native-like conformation to be edited by TAPBPR. Our results demonstrate an inverse relationship between MHC-I peptide occupancy and TAPBPR binding affinity, wherein the lifetime and structural features of transiently bound peptides control the regulation of a conformational switch located near the TAPBPR binding site, which triggers TAPBPR release. These results suggest a similar mechanism for the function of tapasin in the peptide-loading complex.


Authors: Flores-Solis, D., McShan, A., Sgourakis, N.
Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle.,McShan AC, Natarajan K, Kumirov VK, Flores-Solis D, Jiang J, Badstubner M, Toor JS, Bagshaw CR, Kovrigin EL, Margulies DH, Sgourakis NG Nat Chem Biol. 2018 Jul 9. pii: 10.1038/s41589-018-0096-2. doi:, 10.1038/s41589-018-0096-2. PMID:29988068<ref>PMID:29988068</ref>


Description: Solution NMR Structure of Unbound P18-I10
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Mcshan, A]]
<div class="pdbe-citations 6b9k" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Flores-Solis, D]]
[[Category: McShan, A]]
[[Category: Sgourakis, N]]
[[Category: Sgourakis, N]]
[[Category: Flores-Solis, D]]
[[Category: Peptide binding protein]]
[[Category: Structure from cyana 2 1]]
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