6mi4: Difference between revisions
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==Structure of the I65M mutant of NEMO(51-112) with N- and C-terminal coiled-coil adaptors.== | |||
<StructureSection load='6mi4' size='340' side='right'caption='[[6mi4]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mi4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MI4 FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mi3|6mi3]]</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=6mi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mi4 OCA], [http://pdbe.org/6mi4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mi4 RCSB], [http://www.ebi.ac.uk/pdbsum/6mi4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mi4 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
NEMO is an essential component in the activation of the canonical NF-kappaB pathway and exerts its function by recruiting the IkappaB kinases (IKK) to the IKK complex. Inhibition of the NEMO/IKKs interaction is an attractive therapeutic paradigm for diseases related to NF-kappaB mis-regulation, but a difficult endeavor because of the extensive protein-protein interface. Here we report the high-resolution structure of the unbound IKKbeta-binding domain of NEMO that will greatly facilitate the design of NEMO/IKK inhibitors. The structures of unbound NEMO show a closed conformation that partially occludes the three binding hot-spots and suggest a facile transition to an open state that can accommodate ligand binding. By fusing coiled-coil adaptors to the IKKbeta-binding domain of NEMO, we succeeded in creating a protein with improved solution behavior, IKKbeta-binding affinity and crystallization compatibility, which will enable the structural characterization of new NEMO/inhibitor complexes. | |||
The IKK-binding domain of NEMO is an irregular coiled coil with a dynamic binding interface.,Barczewski AH, Ragusa MJ, Mierke DF, Pellegrini M Sci Rep. 2019 Feb 27;9(1):2950. doi: 10.1038/s41598-019-39588-2. PMID:30814588<ref>PMID:30814588</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6mi4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Barczewski, A H]] | |||
[[Category: Mierke, D F]] | |||
[[Category: Pellegrini, M]] | |||
[[Category: Ragusa, M J]] | |||
[[Category: Coiled coil]] | |||
[[Category: Nf-kb pathway]] | |||
[[Category: Scaffolding]] | |||
[[Category: Transcription]] | |||
Revision as of 05:53, 7 August 2019
Structure of the I65M mutant of NEMO(51-112) with N- and C-terminal coiled-coil adaptors.
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