6y7v
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Crystal structure of the KDEL receptor bound to HDEL peptide at pH 6.0== |
| - | <StructureSection load='6y7v' size='340' side='right'caption='[[6y7v]]' scene=''> | + | <StructureSection load='6y7v' size='340' side='right'caption='[[6y7v]], [[Resolution|resolution]] 2.24Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6y7v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y7V FirstGlance]. <br> |
| - | </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=6y7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y7v OCA], [https://pdbe.org/6y7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y7v RCSB], [https://www.ebi.ac.uk/pdbsum/6y7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y7v ProSAT]</span></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]] 2.241Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</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=6y7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y7v OCA], [https://pdbe.org/6y7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y7v RCSB], [https://www.ebi.ac.uk/pdbsum/6y7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y7v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ERD22_CHICK ERD22_CHICK] Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor recognizes K-D-E-L (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ER proteins of widely differing abundance are retrieved from the Golgi by the KDEL-receptor. Abundant ER proteins tend to have KDEL rather than HDEL signals, whereas ADEL and DDEL are not used in most organisms. Here, we explore the mechanism of selective retrieval signal capture by the KDEL-receptor and how HDEL binds with 10-fold higher affinity than KDEL. Our results show the carboxyl-terminus of the retrieval signal moves along a ladder of arginine residues as it enters the binding pocket of the receptor. Gatekeeper residues D50 and E117 at the entrance of this pocket exclude ADEL and DDEL sequences. D50N/E117Q mutation of human KDEL-receptors changes the selectivity to ADEL and DDEL. However, further analysis of HDEL, KDEL, and RDEL-bound receptor structures shows that affinity differences are explained by interactions between the variable -4 H/K/R position of the signal and W120, rather than D50 or E117. Together, these findings explain KDEL-receptor selectivity, and how signal variants increase dynamic range to support efficient ER retrieval of low and high abundance proteins. | ||
| + | |||
| + | A signal capture and proofreading mechanism for the KDEL-receptor explains selectivity and dynamic range in ER retrieval.,Gerondopoulos A, Brauer P, Sobajima T, Wu Z, Parker JL, Biggin PC, Barr FA, Newstead S Elife. 2021 Jun 17;10:e68380. doi: 10.7554/eLife.68380. PMID:34137369<ref>PMID:34137369</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6y7v" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Gallus gallus]] | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Braeuer P]] |
| + | [[Category: Newstead S]] | ||
Current revision
Crystal structure of the KDEL receptor bound to HDEL peptide at pH 6.0
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