5cek: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='5cek' size='340' side='right'caption='[[5cek]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='5cek' size='340' side='right'caption='[[5cek]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5cek]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CEK FirstGlance]. <br>
<table><tr><td colspan='2'>[[5cek]] 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=5CEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CEK FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cem|5cem]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRIB1, C8FW, GIG2, TRB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cek OCA], [https://pdbe.org/5cek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cek RCSB], [https://www.ebi.ac.uk/pdbsum/5cek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cek ProSAT]</span></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=5cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cek OCA], [http://pdbe.org/5cek PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cek RCSB], [http://www.ebi.ac.uk/pdbsum/5cek PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cek ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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> 
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cek" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mace, P D]]
[[Category: Mace PD]]
[[Category: Nakatani, Y]]
[[Category: Nakatani Y]]
[[Category: Kinase]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/5cek"