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6m6o
From Proteopedia
(Difference between revisions)
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<StructureSection load='6m6o' size='340' side='right'caption='[[6m6o]]' scene=''> | <StructureSection load='6m6o' size='340' side='right'caption='[[6m6o]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[6m6o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M6O 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=6m6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m6o OCA], [https://pdbe.org/6m6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m6o RCSB], [https://www.ebi.ac.uk/pdbsum/6m6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m6o 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=6m6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m6o OCA], [https://pdbe.org/6m6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m6o RCSB], [https://www.ebi.ac.uk/pdbsum/6m6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m6o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/CFLAR_HUMAN CFLAR_HUMAN]] Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity.<ref>PMID:9880531</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The formation of death-inducing signaling complex (DISC) and death effector domain (DED) filament initiates extrinsic apoptosis. Recruitment and activation of procaspase-8 at the DISC are regulated by c-FLIP. The interaction between c-FLIP and procaspase-8 is mediated by their tandem DEDs (tDED). However, the structure of c-FLIP(tDED) and how c-FLIP interferes with procaspase-8 activation at the DISC remain elusive. Here, we solved the monomeric structure of c-FLIP(tDED) (F114G) at near physiological pH by solution nuclear magnetic resonance (NMR). Structural superimposition reveals c-FLIP(tDED) (F114G) adopts a structural topology similar to that of procaspase-8(tDED). Our results provide a structural basis for understanding how c-FLIP interacts with procaspase-8 and the molecular mechanisms of c-FLIP in regulating cell death. | ||
| + | |||
| + | Solution structure of c-FLIP death effector domains.,Bai ZQ, Ma X, Liu B, Huang T, Hu K Biochem Biophys Res Commun. 2022 Aug 30;617(Pt 2):1-6. doi:, 10.1016/j.bbrc.2022.05.086. Epub 2022 May 29. PMID:35688044<ref>PMID:35688044</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6m6o" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bai ZQ]] | [[Category: Bai ZQ]] | ||
[[Category: Hu KF]] | [[Category: Hu KF]] | ||
Revision as of 06:24, 28 September 2022
NMR SOLUTION STRUCTURE OF A C-FLIPs
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