View source for 7jya


==Crystal structure of E3 ligase in complex with peptide==
<StructureSection load='7jya' size='340' side='right'caption='[[7jya]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7jya]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JYA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.46&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=7jya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jya OCA], [https://pdbe.org/7jya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jya RCSB], [https://www.ebi.ac.uk/pdbsum/7jya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jya ProSAT]</span></td></tr>
</table>
== 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteome integrity depends on the ubiquitin-proteasome system to degrade unwanted or abnormal proteins. In addition to the N-degrons, C-terminal residues of proteins can also serve as degradation signals (C-degrons) that are recognized by specific cullin-RING ubiquitin ligases (CRLs) for proteasomal degradation. FEM1C is a CRL2 substrate receptor that targets the C-terminal arginine degron (Arg/C-degron), but the molecular mechanism of substrate recognition remains largely elusive. Here, we present crystal structures of FEM1C in complex with Arg/C-degron and show that FEM1C utilizes a semi-open binding pocket to capture the C-terminal arginine and that the extreme C-terminal arginine is the major structural determinant in recognition by FEM1C. Together with biochemical and mutagenesis studies, we provide a framework for understanding molecular recognition of the Arg/C-degron by the FEM family of proteins.

Molecular basis for ubiquitin ligase CRL2(FEM1C)-mediated recognition of C-degron.,Yan X, Wang X, Li Y, Zhou M, Li Y, Song L, Mi W, Min J, Dong C Nat Chem Biol. 2021 Jan 4. pii: 10.1038/s41589-020-00703-4. doi:, 10.1038/s41589-020-00703-4. PMID:33398170<ref>PMID:33398170</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7jya" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Bountra C]]
[[Category: Dong A]]
[[Category: Dong C]]
[[Category: Edwards AM]]
[[Category: Min JR]]
[[Category: Yan X]]