7lxc
From Proteopedia
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==Structure and Interactions of DED1 of human cFLIP== | ==Structure and Interactions of DED1 of human cFLIP== | ||
| - | <StructureSection load='7lxc' size='340' side='right'caption='[[7lxc]]' scene=''> | + | <StructureSection load='7lxc' size='340' side='right'caption='[[7lxc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[7lxc]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LXC FirstGlance]. <br> |
</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=7lxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxc OCA], [https://pdbe.org/7lxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxc RCSB], [https://www.ebi.ac.uk/pdbsum/7lxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxc ProSAT]</span></td></tr> | </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=7lxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lxc OCA], [https://pdbe.org/7lxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lxc RCSB], [https://www.ebi.ac.uk/pdbsum/7lxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lxc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cellular FLICE-like inhibitory protein (cFLIP) is a member of the Death Domain superfamily with pivotal roles in many cellular processes and disease states, including cancer and autoimmune disorders. In the context of the death-inducing signaling complex (DISC), cFLIP isoforms regulate extrinsic apoptosis by controlling procaspase-8 activation. The function of cFLIP is mediated through a series of protein-protein interactions, engaging the two N-terminal death effector domains (DEDs). Here, we solve the structure of an engineered DED1 domain of cFLIP using solution nuclear magnetic resonance (NMR) and we define the interaction with FADD and calmodulin, protein-protein interactions that regulate the function of cFLIP in the DISC. cFLIP DED1 assumes a canonical DED fold characterized by six alpha helices and is able to bind calmodulin and FADD through two separate interfaces. Our results clearly demonstrate the role of DED1 in the cFLIP/FADD association and contribute to the understanding of the assembly of DISC filaments. | ||
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| + | An engineered construct of cFLIP provides insight into DED1 structure and interactions.,Panaitiu AE, Basiashvili T, Mierke DF, Pellegrini M Structure. 2021 Nov 13. pii: S0969-2126(21)00379-8. doi:, 10.1016/j.str.2021.10.011. PMID:34800372<ref>PMID:34800372</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7lxc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Basiashvili T]] | + | [[Category: Basiashvili, T]] |
| - | [[Category: Mierke | + | [[Category: Mierke, D F]] |
| - | [[Category: Panaitiu | + | [[Category: Panaitiu, A E]] |
| - | [[Category: Pellegrini M]] | + | [[Category: Pellegrini, M]] |
| + | [[Category: Apoptosis]] | ||
| + | [[Category: Cflip]] | ||
| + | [[Category: Chimera]] | ||
| + | [[Category: Death effector domain]] | ||
| + | [[Category: Ded1]] | ||
| + | [[Category: Protein binding]] | ||
Revision as of 11:03, 16 February 2022
Structure and Interactions of DED1 of human cFLIP
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