6ldp

<table><tr><td colspan='2'>[[6ldp]] 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=6LDP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LDP 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">CDK5R1, CDK5R, NCK5A ([http://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=6ldp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ldp OCA], [http://pdbe.org/6ldp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ldp RCSB], [http://www.ebi.ac.uk/pdbsum/6ldp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ldp ProSAT]</span></td></tr>

[[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.

<div style="background-color:#fffaf0;">

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.

 

 

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

[[Category: Human]]

[[Category: Chen, X]]

[[Category: Liao, S]]

[[Category: Xu, C]]

[[Category: Ubiquitination e3 ligase]]