2f1s

<table><tr><td colspan='2'>[[2f1s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mcv1 Mcv1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F1S 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=2f1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1s OCA], [https://pdbe.org/2f1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f1s RCSB], [https://www.ebi.ac.uk/pdbsum/2f1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f1s ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/CFLA_MCV1 CFLA_MCV1]] Inhibits TNFRSF1A, TNFRSF6 and TNFRSF12 induced apoptosis. May interfere with caspase-8 recruitment and activation at the death-inducing signaling complex (DISC). May lead to higher virus production and contribute to virus persistence and oncogenicity.<ref>PMID:9087414</ref> <ref>PMID:9037025</ref>

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== Publication Abstract from PubMed ==

Death receptor signaling is initiated by the assembly of the death-inducing signaling complex, which culminates in the activation of the initiator caspase, either caspase-8 or caspase-10. A family of viral and cellular proteins, known as FLIP, plays an essential role in the regulation of death receptor signaling. Viral FLIP (v-FLIP) and short cellular FLIP (c-FLIPS) inhibit apoptosis by interfering with death receptor signaling. The structure and mechanisms of v-FLIP and c-FLIPS remain largely unknown. Here we report a high resolution crystal structure of MC159, a v-FLIP derived from the molluscum contagiosum virus, which is a member of the human poxvirus family. Unexpectedly, the two tandem death effector domains (DEDs) of MC159 rigidly associate with each other through a hydrophobic interface. Structure-based sequence analysis suggests that this interface is conserved in the tandem DEDs from other v-FLIP, c-FLIPS, and caspase-8 and -10. Strikingly, the overall packing arrangement between the two DEDs of MC159 resembles that between the caspase recruitment domains of Apaf-1 and caspase-9. In addition, each DED of MC159 contains a highly conserved binding motif on the surface, to which loss-of-function mutations in MC159 map. These observations, in conjunction with published evidence, reveal significant insights into the function of v-FLIP and suggest a mechanism by which v-FLIP and c-FLIPS inhibit death receptor signaling.

Crystal structure of a viral FLIP: insights into FLIP-mediated inhibition of death receptor signaling.,Li FY, Jeffrey PD, Yu JW, Shi Y J Biol Chem. 2006 Feb 3;281(5):2960-8. Epub 2005 Nov 29. PMID:16317000<ref>PMID:16317000</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2f1s" style="background-color:#fffaf0;"></div>

[[Category: Mcv1]]

[[Category: Jeffrey, P D]]

[[Category: Li, F Y]]

[[Category: Shi, Y]]

[[Category: Yu, J W]]

[[Category: Flip]]