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3qd2
From Proteopedia
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| - | [[Image:3qd2.png|left|200px]] | ||
| - | < | + | ==Crystal structure of mouse PERK kinase domain== |
| - | + | <StructureSection load='3qd2' size='340' side='right'caption='[[3qd2]], [[Resolution|resolution]] 2.81Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3qd2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | |
| - | - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Eif2ak3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/E2AK3_MOUSE E2AK3_MOUSE]] Phosphorylates the alpha subunit of eukaryotic translation-initiation factor 2 (EIF2), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1).<ref>PMID:11035797</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3qd2" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Large Structures]] |
| - | + | [[Category: Lk3 transgenic mice]] | |
| - | + | ||
| - | == | + | |
| - | < | + | |
| - | [[Category: | + | |
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
| - | [[Category: Bingdong, S | + | [[Category: Bingdong, S]] |
| - | [[Category: David, R | + | [[Category: David, R]] |
| - | [[Category: Jingzhi, L | + | [[Category: Jingzhi, L]] |
| - | [[Category: Wenjun, C | + | [[Category: Wenjun, C]] |
[[Category: Eif2a kinase]] | [[Category: Eif2a kinase]] | ||
[[Category: Gene regulation]] | [[Category: Gene regulation]] | ||
[[Category: Phosphoryalation]] | [[Category: Phosphoryalation]] | ||
Current revision
Crystal structure of mouse PERK kinase domain
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