We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

3e7o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:59, 30 August 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3e7o.png|left|200px]]
 
-
<!--
+
==Crystal Structure of JNK2==
-
The line below this paragraph, containing "STRUCTURE_3e7o", creates the "Structure Box" on the page.
+
<StructureSection load='3e7o' size='340' side='right'caption='[[3e7o]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3e7o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E7O FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=35F:N-{3-[5-(1H-1,2,4-TRIAZOL-3-YL)-1H-INDAZOL-3-YL]PHENYL}FURAN-2-CARBOXAMIDE'>35F</scene></td></tr>
-
{{STRUCTURE_3e7o| PDB=3e7o | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e7o OCA], [https://pdbe.org/3e7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e7o RCSB], [https://www.ebi.ac.uk/pdbsum/3e7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e7o ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MK09_HUMAN MK09_HUMAN] Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2. In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels. Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption. When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway. Participates also in neurite growth in spiral ganglion neurons.<ref>PMID:10376527</ref> <ref>PMID:15805466</ref> <ref>PMID:17525747</ref> <ref>PMID:19675674</ref> <ref>PMID:20595622</ref> <ref>PMID:21364637</ref> MAPK9 isoforms display different binding patterns: alpha-1 and alpha-2 preferentially bind to JUN, whereas beta-1 and beta-2 bind to ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms. JUNB is not a substrate for JNK2 alpha-2, and JUND binds only weakly to it.<ref>PMID:10376527</ref> <ref>PMID:15805466</ref> <ref>PMID:17525747</ref> <ref>PMID:19675674</ref> <ref>PMID:20595622</ref> <ref>PMID:21364637</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e7/3e7o_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3e7o ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
c-Jun N-terminal kinase (JNK) 2 is a member of the mitogen-activated protein (MAP) kinase group of signaling proteins. MAP kinases share a common sequence insertion called "MAP kinase insert", which, for ERK2, has been shown to interact with regulatory proteins and, for p38alpha, has been proposed to be involved in the regulation of catalytic activity. We have determined the crystal structure of human JNK2 complexed with an indazole inhibitor by applying a high-throughput protein engineering and surface-site mutagenesis approach. A novel conformation of the activation loop is observed, which is not compatible with its phosphorylation by upstream kinases. This activation inhibitory conformation of JNK2 is stabilized by the MAP kinase insert that interacts with the activation loop in an induced-fit manner. We therefore suggest that the MAP kinase insert of JNK2 plays a role in the regulation of JNK2 activation, possibly by interacting with intracellular binding partners.
-
===Crystal Structure of JNK2===
+
The crystal structure of JNK2 reveals conformational flexibility in the MAP kinase insert and indicates its involvement in the regulation of catalytic activity.,Shaw D, Wang SM, Villasenor AG, Tsing S, Walter D, Browner MF, Barnett J, Kuglstatter A J Mol Biol. 2008 Nov 21;383(4):885-93. Epub 2008 Sep 10. PMID:18801372<ref>PMID:18801372</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3e7o" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_18801372}}, adds the Publication Abstract to the page
+
*[[Mitogen-activated protein kinase 3D structures|Mitogen-activated protein kinase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 18801372 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_18801372}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
3E7O is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E7O OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:18801372</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Mitogen-activated protein kinase]]
+
[[Category: Large Structures]]
-
[[Category: Kuglstatter, A.]]
+
[[Category: Kuglstatter A]]
-
[[Category: Villasenor, A G.]]
+
[[Category: Villasenor AG]]
-
[[Category: Activation loop]]
+
-
[[Category: Alternative splicing]]
+
-
[[Category: Atp-binding]]
+
-
[[Category: Indazole inhibitor]]
+
-
[[Category: Kinase]]
+
-
[[Category: Map kinase insert]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Polymorphism]]
+
-
[[Category: Serine/threonine-protein kinase]]
+
-
[[Category: Transferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jan 18 07:11:14 2010''
+

Current revision

Crystal Structure of JNK2

PDB ID 3e7o

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3e7o"
Personal tools