5v1d

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==Complex structure of the bovine PERK luminal domain and its substrate peptide==
==Complex structure of the bovine PERK luminal domain and its substrate peptide==
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<StructureSection load='5v1d' size='340' side='right' caption='[[5v1d]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='5v1d' size='340' side='right'caption='[[5v1d]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5v1d]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V1D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5v1d]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V1D FirstGlance]. <br>
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</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=5v1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1d OCA], [http://pdbe.org/5v1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v1d RCSB], [http://www.ebi.ac.uk/pdbsum/5v1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1d ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.799&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5v1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1d OCA], [https://pdbe.org/5v1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v1d RCSB], [https://www.ebi.ac.uk/pdbsum/5v1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1d ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A5D791_BOVIN A5D791_BOVIN]
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PRKR-like endoplasmic reticulum kinase (PERK) is one of the major sensor proteins that detect protein folding imbalances during endoplasmic reticulum (ER) stress. However, it remains unclear how ER stress activates PERK to initiate a downstream unfolded protein response (UPR). Here, we found that PERK's luminal domain can recognize and selectively interact with misfolded proteins but not with native proteins. Screening a phage-display library, we identified a peptide substrate, P16, of the PERK luminal domain and confirmed that P16 efficiently competes with misfolded proteins for binding this domain. To unravel the mechanism by which the PERK luminal domain interacts with misfolded proteins, we determined the crystal structure of the bovine PERK luminal domain complexed with P16 to 2.8 A resolution. The structure revealed that PERK's luminal domain binds the peptide through a conserved hydrophobic groove. Substitutions within hydrophobic regions of the PERK luminal domain abolished the binding between PERK and misfolded proteins. We also noted that peptide binding results in major conformational changes in the PERK luminal domain which may favor PERK oligomerization. The structure of the PERK luminal domain-P16 complex suggested stacking of the luminal domain that leads to PERK oligomerization and activation via autophosphorylation after ligand binding. Collectively, our structural and biochemical results strongly support a ligand-driven model in which the PERK luminal domain interacts directly with misfolded proteins to induce PERK oligomerization and activation, resulting in ER stress signaling and the UPR.
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The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization.,Wang P, Li J, Tao J, Sha B J Biol Chem. 2018 Jan 31. pii: RA117.001294. doi: 10.1074/jbc.RA117.001294. PMID:29386355<ref>PMID:29386355</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5v1d" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Li, J]]
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[[Category: Bos taurus]]
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[[Category: Sha, B]]
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[[Category: Large Structures]]
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[[Category: Wang, P]]
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[[Category: Synthetic construct]]
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[[Category: Complex structure]]
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[[Category: Li J]]
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[[Category: Luminal domain]]
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[[Category: Sha B]]
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[[Category: Perk]]
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[[Category: Wang P]]
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[[Category: Substrate peptide]]
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[[Category: Transferase-substrate complex]]
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Current revision

Complex structure of the bovine PERK luminal domain and its substrate peptide

PDB ID 5v1d

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