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| | <StructureSection load='6lf0' size='340' side='right'caption='[[6lf0]], [[Resolution|resolution]] 2.11Å' scene=''> | | <StructureSection load='6lf0' size='340' side='right'caption='[[6lf0]], [[Resolution|resolution]] 2.11Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6lf0]] 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=6LF0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LF0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6lf0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LF0 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11Å</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> | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lf0 OCA], [http://pdbe.org/6lf0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lf0 RCSB], [http://www.ebi.ac.uk/pdbsum/6lf0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lf0 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=6lf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lf0 OCA], [https://pdbe.org/6lf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lf0 RCSB], [https://www.ebi.ac.uk/pdbsum/6lf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lf0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, X]] | + | [[Category: Chen X]] |
| - | [[Category: Liao, S]] | + | [[Category: Liao S]] |
| - | [[Category: Xu, C]] | + | [[Category: Xu C]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Ubiquitination e3 ligase]]
| + | |
| Structural highlights
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
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