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5cem

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==Pseudokinase and C-terminal extension of Human Tribbles Homolog 1==
==Pseudokinase and C-terminal extension of Human Tribbles Homolog 1==
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<StructureSection load='5cem' size='340' side='right' caption='[[5cem]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='5cem' size='340' side='right'caption='[[5cem]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5cem]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CEM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CEM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5cem]] is a 1 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=5CEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CEM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cek|5cek]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=5cem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cem OCA], [http://pdbe.org/5cem PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cem RCSB], [http://www.ebi.ac.uk/pdbsum/5cem PDBsum]</span></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=5cem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cem OCA], [https://pdbe.org/5cem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cem RCSB], [https://www.ebi.ac.uk/pdbsum/5cem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cem ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TRIB1_HUMAN TRIB1_HUMAN]] Interacts with MAPK kinases and regulates activation of MAP kinases. May not display kinase activity.<ref>PMID:15299019</ref> <ref>PMID:15299019</ref>
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[https://www.uniprot.org/uniprot/TRIB1_HUMAN TRIB1_HUMAN] Interacts with MAPK kinases and regulates activation of MAP kinases. May not display kinase activity.<ref>PMID:15299019</ref> <ref>PMID:15299019</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CCAAT-enhancer binding proteins (C/EBPs) are transcription factors that play a central role in the differentiation of myeloid cells and adipocytes. Tribbles pseudokinases govern levels of C/EBPs by recruiting them to the COP1 ubiquitin ligase for ubiquitination. Here, we present the first crystal structure of a Tribbles protein, which reveals a catalytically inactive TRIB1 pseudokinase domain with a unique adaptation in the alphaC helix. A second crystal structure and biophysical studies of TRIB1 with its C-terminal extension, which includes the COP1-binding motif, show that the C-terminal extension is sequestered at a site formed by the modified TRIB1 alphaC helix. In addition, we have identified and characterized the TRIB1 substrate-recognition sequence within C/EBPalpha, which is evolutionarily conserved in C/EBP transcription factors. Binding studies indicate that C/EBPalpha recruitment is weaker in the presence of the C-terminal COP1-binding motif, but the magnitude of this effect suggests that the two bind distinct rather directly overlapping binding sites.
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Molecular Mechanism of CCAAT-Enhancer Binding Protein Recruitment by the TRIB1 Pseudokinase.,Murphy JM, Nakatani Y, Jamieson SA, Dai W, Lucet IS, Mace PD Structure. 2015 Nov 3;23(11):2111-21. doi: 10.1016/j.str.2015.08.017. Epub 2015, Oct 9. PMID:26455797<ref>PMID:26455797</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 5cem" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mace, P D]]
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[[Category: Homo sapiens]]
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[[Category: Nakatani, Y]]
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[[Category: Large Structures]]
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[[Category: Kinase]]
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[[Category: Mace PD]]
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[[Category: Kinase-like]]
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[[Category: Nakatani Y]]
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[[Category: Transferase]]
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Current revision

Pseudokinase and C-terminal extension of Human Tribbles Homolog 1

PDB ID 5cem

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