6lbf

From Proteopedia

(Difference between revisions)

Revision as of 17:44, 10 March 2021

Crystal structure of FEM1B

Structural highlights

6lbf is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	FEM1B, F1AA, KIAA0396 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FEM1B_HUMAN] Component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. Involved in apoptosis by acting as a death receptor-associated protein that mediates apoptosis. Also involved in glucose homeostasis in pancreatic islet. Functions as an adapter/mediator in replication stress-induced signaling that leads to the activation of CHEK1.^[1] ^[2]

Publication Abstract from PubMed

Degrons are elements within protein substrates that mediate the interaction with specific degradation machineries to control proteolysis. Recently, a few classes of C-terminal degrons (C-degrons) that are recognized by dedicated cullin-RING ligases (CRLs) have been identified. Specifically, CRL2 using the related substrate adapters FEM1A/B/C was found to recognize C degrons ending with arginine (Arg/C-degron). Here, we uncover the molecular mechanism of Arg/C-degron recognition by solving a subset of structures of FEM1 proteins in complex with Arg/C-degron-bearing substrates. Our structural research, complemented by binding assays and global protein stability (GPS) analyses, demonstrates that FEM1A/C and FEM1B selectively target distinct classes of Arg/C-degrons. Overall, our study not only sheds light on the molecular mechanism underlying Arg/C-degron recognition for precise control of substrate turnover, but also provides valuable information for development of chemical probes for selectively regulating proteostasis.

Molecular basis for arginine C-terminal degron recognition by Cul2(FEM1) E3 ligase.,Chen X, Liao S, Makaros Y, Guo Q, Zhu Z, Krizelman R, Dahan K, Tu X, Yao X, Koren I, Xu C Nat Chem Biol. 2021 Jan 4. pii: 10.1038/s41589-020-00704-3. doi:, 10.1038/s41589-020-00704-3. PMID:33398168^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chan SL, Tan KO, Zhang L, Yee KS, Ronca F, Chan MY, Yu VC. F1Aalpha, a death receptor-binding protein homologous to the Caenorhabditis elegans sex-determining protein, FEM-1, is a caspase substrate that mediates apoptosis. J Biol Chem. 1999 Nov 5;274(45):32461-8. PMID:10542291
↑ Sun TP, Shieh SY. Human FEM1B is required for Rad9 recruitment and CHK1 activation in response to replication stress. Oncogene. 2009 May 7;28(18):1971-81. doi: 10.1038/onc.2009.58. Epub 2009 Mar 30. PMID:19330022 doi:http://dx.doi.org/10.1038/onc.2009.58
↑ Chen X, Liao S, Makaros Y, Guo Q, Zhu Z, Krizelman R, Dahan K, Tu X, Yao X, Koren I, Xu C. Molecular basis for arginine C-terminal degron recognition by Cul2(FEM1) E3 ligase. Nat Chem Biol. 2021 Jan 4. pii: 10.1038/s41589-020-00704-3. doi:, 10.1038/s41589-020-00704-3. PMID:33398168 doi:http://dx.doi.org/10.1038/s41589-020-00704-3

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6lbf"

@@ Line 3: / Line 3: @@
 <StructureSection load='6lbf' size='340' side='right'caption='[[6lbf]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6lbf]] is a 2 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=6LBF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LBF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6lbf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LBF FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FEM1B, F1AA, KIAA0396 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FEM1B, F1AA, KIAA0396 ([https://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'>[http://proteopedia.org/fgij/fg.htm?mol=6lbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lbf OCA], [http://pdbe.org/6lbf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lbf RCSB], [http://www.ebi.ac.uk/pdbsum/6lbf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lbf ProSAT]</span></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=6lbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lbf OCA], [https://pdbe.org/6lbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lbf RCSB], [https://www.ebi.ac.uk/pdbsum/6lbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lbf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FEM1B_HUMAN FEM1B_HUMAN]] Component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. Involved in apoptosis by acting as a death receptor-associated protein that mediates apoptosis. Also involved in glucose homeostasis in pancreatic islet. Functions as an adapter/mediator in replication stress-induced signaling that leads to the activation of CHEK1.<ref>PMID:10542291</ref> <ref>PMID:19330022</ref>
+[[https://www.uniprot.org/uniprot/FEM1B_HUMAN FEM1B_HUMAN]] Component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. Involved in apoptosis by acting as a death receptor-associated protein that mediates apoptosis. Also involved in glucose homeostasis in pancreatic islet. Functions as an adapter/mediator in replication stress-induced signaling that leads to the activation of CHEK1.<ref>PMID:10542291</ref> <ref>PMID:19330022</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

6lbf

From Proteopedia

Revision as of 17:44, 10 March 2021

Crystal structure of FEM1B

Structural highlights

Function

Publication Abstract from PubMed

References

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