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5h7r
From Proteopedia
(Difference between revisions)
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<StructureSection load='5h7r' size='340' side='right' caption='[[5h7r]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5h7r' size='340' side='right' caption='[[5h7r]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5h7r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H7R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H7R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h7r]] is a 1 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=5H7R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H7R 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h7s|5h7s]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h7s|5h7s]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LNX1, LNX, PDZRN2, UNQ574/PRO1136 ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5h7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h7r OCA], [http://pdbe.org/5h7r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h7r RCSB], [http://www.ebi.ac.uk/pdbsum/5h7r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h7r 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=5h7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h7r OCA], [http://pdbe.org/5h7r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h7r RCSB], [http://www.ebi.ac.uk/pdbsum/5h7r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h7r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/LNX1_HUMAN LNX1_HUMAN]] E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65 (By similarity). Isoform 2 provides an endocytic scaffold for IGSF5/JAM4 (By similarity). | [[http://www.uniprot.org/uniprot/LNX1_HUMAN LNX1_HUMAN]] E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65 (By similarity). Isoform 2 provides an endocytic scaffold for IGSF5/JAM4 (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | LNX1 (Ligand of Numb Protein-X 1) is a RING and PDZ domain-containing E3 ubiquitin ligase that ubiquitinates human c-Src kinase. Here, we report the identification and structure of the ubiquitination domain of LNX1, the identification of Ubc13/Ube2V2 as a functional E2 in vitro, and the structural and functional studies of the Ubc13~Ub intermediate in complex with the ubiquitination domain of LNX1. The RING domain of LNX1 is embedded between two zinc-finger motifs (Zn-RING-Zn), both of which are crucial for its ubiquitination activity. In the heterodimeric complex, the ubiquitin of one monomer shares more buried surface area with LNX1 of the other monomer and these interactions are unique and essential for catalysis. This study reveals how the LNX1 RING domain is structurally and mechanistically dependent on other motifs for its E3 ligase activity, and describes how dimeric LNX1 recruits ubiquitin-loaded Ubc13 for Ub transfer via E3 ligase-mediated catalysis. | ||
| + | |||
| + | Structure of LNX1:Ubc13~Ubiquitin complex reveals the role of additional motifs for the E3 ligase activity of LNX1.,Nayak D, Sivaraman J J Mol Biol. 2018 Feb 26. pii: S0022-2836(18)30089-5. doi:, 10.1016/j.jmb.2018.02.016. PMID:29496391<ref>PMID:29496391</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5h7r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Nayak, D]] | [[Category: Nayak, D]] | ||
[[Category: Sivaraman, J]] | [[Category: Sivaraman, J]] | ||
Revision as of 06:47, 14 March 2018
Structural basis of the flanking zinc-finger motifs crucial for the E3 ligase activity of the LNX1 RING domain
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Categories: Human | Nayak, D | Sivaraman, J | E3 ligase | Ligase | Ring | Ubiquitination | Zn finger motif
