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6len

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Revision as of 17:44, 10 March 2021

Structure of NS11 bound FEM1C

Structural highlights

6len 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.
Gene:	FEM1C, KIAA1785 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FEM1C_HUMAN] Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit.

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^[1]

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

References

↑ 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/6len"

@@ Line 3: / Line 3: @@
 <StructureSection load='6len' size='340' side='right'caption='[[6len]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6len]] 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=6LEN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LEN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6len]] 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=6LEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LEN FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FEM1C, KIAA1785 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FEM1C, KIAA1785 ([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=6len FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6len OCA], [http://pdbe.org/6len PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6len RCSB], [http://www.ebi.ac.uk/pdbsum/6len PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6len 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=6len FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6len OCA], [https://pdbe.org/6len PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6len RCSB], [https://www.ebi.ac.uk/pdbsum/6len PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6len ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FEM1C_HUMAN FEM1C_HUMAN]] Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit.
+[[https://www.uniprot.org/uniprot/FEM1C_HUMAN FEM1C_HUMAN]] Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

6len

From Proteopedia

Revision as of 17:44, 10 March 2021

Structure of NS11 bound FEM1C

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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