5zi6: Difference between revisions
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<StructureSection load='5zi6' size='340' side='right' caption='[[5zi6]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5zi6' size='340' side='right' caption='[[5zi6]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5zi6]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZI6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5zi6]] is a 8 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=5ZI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZI6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MEX3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zi6 OCA], [http://pdbe.org/5zi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5zi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zi6 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zi6 OCA], [http://pdbe.org/5zi6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zi6 RCSB], [http://www.ebi.ac.uk/pdbsum/5zi6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zi6 ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: RING-type E3 ubiquitin transferase]] | [[Category: RING-type E3 ubiquitin transferase]] | ||
[[Category: Moududee, S A]] | [[Category: Moududee, S A]] | ||
Revision as of 15:35, 7 November 2018
The RING domain structure of MEX-3CThe RING domain structure of MEX-3C
Structural highlights
Disease[MEX3C_HUMAN] Genetic variations in MEX3C may be associated with susceptibility to essential hypertension.[1] Function[MEX3C_HUMAN] E3 ubiquitin ligase responsible for the post-transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation.[2] [3] Publication Abstract from PubMedMEX-3C, a novel RNA binding E3 ubiquitin ligases, contains two N-terminal heterogeneous nuclear ribonucleoprotein K homology (KH) domains and C-terminal Ring finger domain. Recent evidence has suggested that human MEX-3C has a strong bondage with carcinogenesis and the MEX-3C-mediated ubiquitination of RIG-I is essential for the antiviral innate immune response. Moreover, the Ring finger domain of MEX-3C could regulate the degradation of HLA-A2 (an MHC-I allotype) mRNA with a novel mechanism. However, the structural basis for the ubiquitination catalyzed by hMEX-3C Ring finger domain remains evasive. In this study, we solved the crystal structure of dimeric Ring finger domain of hMEX-3C and compared it with the complex structure of MDM2/MDMX-UbcH5b-Ub. Our ubiquitination assay demonstrated that the Ring finger domain of hMEX-3C acts as a ubiquitin E3 ligase in vitro, cooperating with specific E2 to mediate ubiquitination. Then, we identified several key residues in Ring finger domain of hMEX-3C possibly involved in the interaction with E2-Ub conjugate and analyzed the E3 ligase activities of wild type and mutants at key sites. Additionally, zinc chelation experiments indicated that the intact structural stability is essential for the self-ubiquitination activity of the Ring finger domain of hMEX-3C. Taken together, our studies provided new insight into the mechanism of the Ring finger domain of hMEX-3C that may play an important role in eliciting antiviral immune responses and therapeutic interventions. Structural and functional characterization of hMEX-3C Ring finger domain as an E3 ubiquitin ligase.,Moududee SA, Jiang Y, Gilbert N, Xie G, Xu Z, Wu J, Gong Q, Tang Y, Shi Y Protein Sci. 2018 Sep;27(9):1661-1669. doi: 10.1002/pro.3473. PMID:30095198[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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