View source for 3qd2


==Crystal structure of mouse PERK kinase domain==
<StructureSection load='3qd2' size='340' side='right'caption='[[3qd2]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QD2 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]] 2.81&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=3qd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qd2 OCA], [https://pdbe.org/3qd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qd2 RCSB], [https://www.ebi.ac.uk/pdbsum/3qd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qd2 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The endoplasmic reticulum (ER) unfolded protein response (UPR) is comprised of several intracellular signaling pathways that alleviate ER stress. The ER-localized transmembrane kinase PERK is one of three major ER stress transducers. Oligomerization of PERK's N-terminal ER luminal domain by ER stress promotes PERK trans-autophosphorylation of the C-terminal cytoplasmic kinase domain at multiple residues including Thr980 on the kinase activation loop. Activated PERK phosphorylates Ser51 of the alpha-subunit of translation initiation factor 2 (eIF2alpha), which inhibits initiation of protein synthesis and reduces the load of unfolded proteins entering the ER. The crystal structure of PERK's kinase domain has been determined to 2.8 A resolution. The structure resembles the back-to-back dimer observed in the related eIF2alpha kinase PKR. Phosphorylation of Thr980 stabilizes both the activation loop and helix alphaG in the C-terminal lobe, preparing the latter for eIF2alpha binding. The structure suggests conservation in the mode of activation of eIF2alpha kinases and is consistent with a `line-up' model for PERK activation triggered by oligomerization of its luminal domain.

The structure of the PERK kinase domain suggests the mechanism for its activation.,Cui W, Li J, Ron D, Sha B Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):423-8. Epub 2011 Apr 13. PMID:21543844<ref>PMID:21543844</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3qd2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Bingdong S]]
[[Category: David R]]
[[Category: Jingzhi L]]
[[Category: Wenjun C]]