6lbg: Difference between revisions
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<StructureSection load='6lbg' size='340' side='right'caption='[[6lbg]], [[Resolution|resolution]] 2.51Å' scene=''> | <StructureSection load='6lbg' size='340' side='right'caption='[[6lbg]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6lbg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[6lbg]] 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=6LBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LBG FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51Å</td></tr> | ||
<tr id=' | <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'>[https://proteopedia.org/fgij/fg.htm?mol=6lbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lbg OCA], [https://pdbe.org/6lbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lbg RCSB], [https://www.ebi.ac.uk/pdbsum/6lbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lbg 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=6lbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lbg OCA], [https://pdbe.org/6lbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lbg RCSB], [https://www.ebi.ac.uk/pdbsum/6lbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lbg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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.[https://www.uniprot.org/uniprot/O51B2_HUMAN O51B2_HUMAN] Odorant receptor. | |||
<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: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chen | [[Category: Chen X]] | ||
[[Category: Liao | [[Category: Liao S]] | ||
[[Category: Xu | [[Category: Xu C]] | ||
Latest revision as of 13:55, 22 November 2023
Structure of OR51B2 bound FEM1CStructure of OR51B2 bound FEM1C
Structural highlights
FunctionFEM1C_HUMAN Probable component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit.O51B2_HUMAN Odorant receptor. Publication Abstract from PubMedDegrons 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
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